Professional Documents
Culture Documents
Ehs 207
Ehs 207
GUIDE
Lagos Office
14/16 Ahmadu Bello Way
Victoria Island, Lagos
e-mail: [email protected]
URL: www.nou.edu.ng
Printed 2020
ISBN: 978-978-970-151-3
ii
EHS 207 COURSE GUIDE
CONTENTS PAGE
Introduction……………………………………………. iv
What you will Learn in the Course………………….. iv
Course Aim……………………………………………. v
Course Objective………………………………………. v
Working through the Course…………………………. v
The Course Materials………………………………….. v
Study Units…………………………………………….. v
Presentation Schedule…………………………………. vi
Assessment……………………………………………. vi
Tutor-Marked Assignment……………………………. vii
Course Marking Scheme……………………………… viii
Facilitators/Tutors and Tutorials……………………… viii
Summary……………………………………………… viii
iii
EHS 207 COURSE GUIDE
INTRODUCTION
EHS 207 title “General Biochemistry” is a three (3) Unit course with
four (4) Modules and fifteen (15) Units. Biochemistry is the study of
biomolecules. It can also be defined as the application of chemistry to
the study of biological processes in living organisms. Biochemistry is
both a life science and a chemistry science; it explores the chemistry of
living organisms and the molecular basis for the changes occurring in
living cells.
In this course, you will learn about the branches of biochemistry and its
relevance to other life sciences, biochemistry of living cells, biological
oxidation and electron transport chain, buffer, acidity, alkalinity, pH,
pKa values and their roles in cellular metabolism. You will learn about
the metabolism of biomolecules such as carbohydrate, proteins as well
as lipids. The structure of the DNA will also be discussed. The
knowledge that will be acquired in this course will assist you in
understanding the various biochemical reactions that takes place in the
living system.
iv
EHS 207 COURSE GUIDE
COURSE AIM
COURSE OBJECTIVES
As a student of this course you are expected to register for this course
online which is available at the NOUN website before you can have
access to all the materials. You will be expected to read every module
along with all assigned readings to prepare you for assessment.
Note that each unit has self-assessment exercises which you are advised
to do and at certain periods during the course, you will be expected to
submit your assignment for the purpose of assessment. There will be
final examination
STUDY UNITS
There are four (4) modules and fourteen (14) study units in this course
They are as follows:
v
EHS 207 COURSE GUIDE
There are activities related to the lecture in each unit which will help
your progress and comprehension of the unit. You are required to work
on these exercises which together with the TMAs will enable you to
achieve the objectives of each unit.
PRESENTATION SCHEDULE
There is a time-table prepared for the early and timely completion and
submissions of your TMAs as well as attending the tutorial classes. You
are required to submit all your assignments by the stipulated time and
date. Avoid falling behind the schedule time.
ASSESSMENT
vi
EHS 207 COURSE GUIDE
The work submitted to your tutor for assessment will count for 30% of
your total course work.
At the end of this course, you have to sit for a final or end of course
examination of about a three-hour duration which will count for 70% of
your total course mark.
TUTOR-MARKED ASSIGNMENT
Reading and researching into your references will give you a better
deeper understanding of the subject.
2. You will need to revise the whole course content before sitting
for the examination. The self-assessment activities and TMAs
will be useful for this purpose. The examination concludes the
assessment for the course and constitutes 70% of the whole
course. All areas of the course will be examined and you will be
informed the time for the examination.
vii
EHS 207 COURSE GUIDE
Sixteen (16) hours are provided for tutorials for this course. You will be
notified of the dates, times and location for these tutorial classes. As
soon as you are allocated a tutorial group, the name and phone number
of your facilitator will be given to you. These are the duties of your
facilitator: He or she will mark and comment on your assignment. He
will monitor your progress and provide any necessary assistance you
need. He or she will mark your TMAs and return them to you as soon as
possible.
You should endeavor to attend the tutorials. This is the only chance to
have face to face with your course facilitator and to ask questions which
are answered instantly. You can raise any problem encountered in the
course of your study.
SUMMARY
viii
EHS 207 COURSE GUIDE
You are expected to apply the knowledge you have acquired during this
course to your practical life.
define biochemistry
discuss the metabolism of carbohydrates, proteins and lipids
give an account of oxidative phosphorylation and electron
transport chain
explain the detoxification processes of harmful substances.
ix
MAIN
COURSE
CONTENTS PAGE
CONTENTS
1.0 Introduction
2.0 Objectives
3.0 Main Content
3.1 Definition of Biochemistry
3.2 Relevance of Biochemistry as a Life Science
3.3 Branches of Biochemistry
4.0 Conclusion
5.0 Summary
6.0 Tutor-Marked Assignment
7.0 References/Further Reading
1.0 INTRODUCTION
2.0 OBJECTIVES
define biochemistry
state the relevance of biochemistry to other life sciences (nursing,
medicine, pharmacy)
describe different branches of biochemistry.
1
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
2
EHS 207 MODULE 1
4.0 CONCLUSION
5.0 SUMMARY
3
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
1. Define biochemistry.
2. Name and explain three (3) branches of biochemistry.
3. Discuss the relevance of biochemistry to other life sciences.
Murray, R.K., Bender, D. A., Botham, K., M., Kennelly, P.J., Rodwell
V.W. & Well, P.A. (2012).Harper’s Illustrated Biochemistry
(29thed.).McGraw-HillMedical.
4
EHS 207 MODULE 1
CONTENTS
1.0 Introduction
2.0 Objectives
3.0 Main Content
3.1 Structure of Animal Cell
3.2 Components of the Cell and their Functions
4.0 Conclusion
5.0 Summary
6.0 Tutor-Marked Assignment
7.0 References/Further Reading
1.0 INTRODUCTION
The living cell we are to discuss here is not different from the cell you
learnt in Biology when you were in secondary school. Cells are the basic
building blocks of all living organism. The human body is composed of
trillion of cells. Cells have many parts, each with a different function.
Some of these parts called organelles are specialized structures that
perform certain tasks within the cell. Biochemical arrangement of cells
and how these cells interact to perform various functions in man are not
only fascinating but also very interesting. Imagine the sensitivity of cells
responsible for taste; different region of your tongue detects different
taste.
Some cells are replaced every 72 hours in our body while some spend
up to ten years before they die. Also, some cells remain in our body
throughout our lifetime. There are two basic types of cells in nature and
these are prokaryotic and eukaryotic cells. Prokaryotic cells are the
simplest cells and are without a nucleus and cell organelles while
eukaryotic cells are sophisticated cells with a well-defined nucleus and
cell organelles. A group of cells forms tissue, various tissues forms an
organ and different organs make up the body.
5
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
2.0 OBJECTIVE
discuss the cell, structure of the animal cell, cell organelles and
their functions.
6
EHS 207 MODULE 1
extracellular fluid (ECF) from mixing with the fluid inside the
cell called intracellular fluid (ICF). Plasma membrane regulates
the materials that enters or leaves the cell, for this reason, it is
said to be semi-permeable. In addition, the plasma membrane has
some glycoproteins and glycolipids on its surface; these
molecules serve as signal molecule between cells.
ii. The Cytoplasm: This is the fluid-like space between the plasma
and nuclear membrane. Cytoplasm is the cavity where the
organelles are found. It providesspace for the movement of
synthesised products from one compartment to another for further
processing. The organelles are suspended in the cytoplasm by
cytoskeleton network that resemble nets.
iii. Nucleus: This is the most important part of the cell, the nucleus is
always centrally located. It has its own membrane called nuclear
membrane which protects the content of the nucleus. Nucleus is
very important to the cell because it contains the genetic materials
(DNA and RNA) that control all the activities of the cell. Nucleus
regulates the rate and time of cell division. It also determines the
materials that enter or exit thecell.
7
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
4.0 CONCLUSION
The cell is the structural and functional basic unit of life. The human
body contains several billions of cells that perform various functions.
There are specialized structures called cell organelles present within the
cell through which the cell performs these various functions.
5.0 SUMMARY
In this unit, you have learnt about the cell, types of cells, structure of the
animal cell, cell organelles and their functions.
6.0 TUTOR-MARKEDASSIGNMENT
8
EHS 207 MODULE 1
9
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
CONTENTS
1.0 Introduction
2.0 Objectives
3.0 Main Content
3.1 Components of the Plasma Membrane
3.2 The Functions of Plasma Membranes
3.3 Transportation of Materials across the Plasma Membrane
4.0 Conclusion
5.0 Summary
6.0 Tutor-Marked Assignment
7.0 References/Further Reading
1.0 INTRODUCTION
2.0 OBJECTIVES
10
EHS 207 MODULE 1
Membrane Lipids
Cholesterol
Membrane Proteins
11
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
12
EHS 207 MODULE 1
facilitated diffusion include glucose, amino acids and many small ions.
The movement of water through membranes also involves facilitated
diffusion. The special protein channel used for this is called aquaporins,
and it facilitates the movement of water at a rate needed for cell
activities. Facilitated diffusion process may be coupled to the movement
of other molecules in the same direction or opposite direction. In co-
transport, the transport of one molecule depends on sequential transfer
of another molecule. Co-transport may be symport or antiport. A
symport moves two molecules in the same direction e.g. sodium-glucose
transporter. Antiport system moves two molecules in opposite direction.
It is also known as counter transport e.g. sodium-potassium transporter.
The energy required for the transportation of sodium and potassium ions
are derived from the hydrolysis of ATP. For every three Na+ pumped
out of the cell, two K+ are released into the cytosol.
13
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Fig. 1.3: Active and Passive Transport across the Plasma Membrane
Source: Delvin (2010).
4.0 CONCLUSION
5.0 SUMMARY
In this unit, you have learnt about the lipids and protein components of
the cell membrane. We also discussed the different mechanism of
transportation of material across the cell membrane with explanation of
the factors that drive such exchange.
14
EHS 207 MODULE 1
Murray, R. K., Bender, D. A., Botham, K., M., Kennelly, P.J., Rodwell
V. W. and Well, P. A. (2012). Harper’s Illustrated
th
Biochemistry (29 Edition) McGraw-HillMedical.
15
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
1.0 Introduction
2.0 Objectives
3.0 Main Content
3.1 The Properties of Water
3.2 Biological Importance of Water
3.3 Acid, Base and Buffer
3.4 Biological Importance of buffer
4.0 Conclusion
5.0 Summary
6.0 Tutor-marked Assignment
7.0 References/Further reading
1.0 INTRODUCTION
Water is the most abundant matter on earth and also a major component
of the body. Typically, organisms are constituted of 70 to 90 % water. It
must be present before any metabolic activity can take place in the cell
and it is referred to as a weak electrolyte because it can undergo partial
dissociation into a proton (H+) and hydroxyl ion (OH-).
2.0 OBJECTIVES
At the end of this unit, you should understand the properties of water,
the importance of water as the major component of living organisms and
16
EHS 207 MODULE 2
be able to define acid, base and a buffer. You will also learn how to
calculate pH, pOH and pKa of a given solution.
17
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
HA H+ + A -
Acid may dissociate partially (called weak acid e.g. ethanoic acid,
water) or completely (called strong acid e.g. hydrochloric acid) in
solution. In solution, weak acid establishes equilibrium between the
proton and its conjugate base. Weak acids are those which have a slight
tendency to give up protons e.g. acetic acid. On the other hand, strong
acids give up protons readily e.g. HCl.
HCl H+ + Cl-
CH3COOH CH3COO- + H+
H2 O H+ + OH-
The normal pH of the blood plasma ranges between 7.35 and 7.45,
average being 7.4. The intracellular pH of the tissues is 7.25 to 7.35
averaging to 7.30 and pH of extracellular fluid is 7.30 to 7.40 with an
average of 7.35. A decrease in the pH of blood is termed as acidosis and
an increase in the pH of blood is termed as alkalosis. Alkalosis is more
fatal than acidosis.
18
EHS 207 MODULE 2
Mathematically,
pH = - log [H+] and
Ka = = [H+] [A-]
[HA]
Solution:
pH = - log [H+], log[4.2 x 10-3] = log 4.2 + log 10-3 = 0.62 -3 = -2.38.
Substitute for log [H+] in the equation.
pH = -(-2.38), the two negative values canceled out, pH = 2.38
Solution:
pH = -log 1.33 x 10-3 = 0.12-3, if you take away 3 from 0.12, this will
give you a negative value (-2.88).
pH = 2.88 .
19
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Buffer
If (H+) hydrogen ions are added to a buffer solution, the conjugate base
reacts with the excess hydrogen ions to form the acid. On the other
hand, if (OH-) hydroxyl ions are added, they react with the acid present
in the buffer to produce water and conjugate base.
Preparation of buffer
20
EHS 207 MODULE 2
4.0 CONCLUSION
Water is life and a core component of all other fluids that make chemical
reactions possible in the body. Acids, bases and buffers serve different
biological purposes in the living system.
5.0 SUMMARY
In this study unit, you have learnt about the properties of water and its
biological importance, acid, base and buffers. You are also introduced to
the Henderson-Hasselbalch equation
21
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Murray, R. K., Bender, D. A., Botham, K., M., Kennelly, P. J., Rodwell
V.W. and Well, P. A. (2012). Harper’s Illustrated
th
Biochemistry (29 edition) McGraw-Hill Medical
22
EHS 207 MODULE 2
1.0 Introduction
2.0 Objectives
3.0 Main Content
3.1 Classification of Carbohydrates
3.2 Isomers of Glucose
3.3 Functions of Carbohydrates
4.0 Conclusion
5.0 Summary
6.0 Tutor-marked Assignments
7.0 References/Further reading
1.0 INTRODUCTION
2.0 OBJECTIVES
At the end of this unit, you should be able to know the classification of
carbohydrates into various sugars, the isomers of glucose and the roles
of carbohydrates in biological membrane.
Monosaccharides: These are sugars that contain one sugar unit and
cannot be further hydrolyzed. They represent the end product of CHO
digestion in the human body. They are classified as trioses, tetroses,
23
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
24
EHS 207 MODULE 2
polymer from plant cell walls) and inulin (a fructose polymer which the
storage CHO in some plants. Examples of polysaccharides are glycogen,
starch and dextrin which may be linear or branched polymers
Structure of Glucose
The straight chain structural formula of glucose can account for some of
its properties, but a cyclic structure formed by a reaction between the
aldehyde group and an OH group is thermodynamically more favoured
and accounts for other properties. The cyclic structure results from the
reaction between the aldehyde group in C1 and the OH group in C5,
which forms a hemiacetal linkage and produce either of 2 stereoisomers.
The structure can also be represented in form of a chair, with the 6
membered rings containing one oxygen atom as shown in Figure 2.3.
25
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
26
EHS 207 MODULE 2
27
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
4.0 CONCLUSION
5.0 SUMMARY
28
EHS 207 MODULE 2
29
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
1.0 Introduction
2.0 Objectives
3.0 Main Content
3.1 Chemical Nature of Amino Acids
3.2 The 20 Amino Acids found in Proteins
3.3 Classification of Amino Acids
3.4 Classification of Proteins
3.5 Roles of Protein in Biological Process
4.0 Conclusion
5.0 Summary
6.0 Tutor-marked Assessment
7.0 References/Further reading
1.0 INTRODUCTION
Amino acids are the basic structural units of proteins. Proteins in all
species from bacteria to humans are made from the same set of twenty
amino acids. Amino acids take part in many types of reactions, but the
most important of these is the formation of a peptide bond. This
involves the joining of the α- carboxyl group of one amino acid to the α-
amino group of another amino acid, with the loss of a water molecule.
Amino acids are grouped according to the nature of their side chains.
Since amino acids are weak acids, their strength is expressed as pKa
(negative log of ionization constant). The net charge on an amino acid
depends on the pKa of its functional groups and the pH of the
surrounding medium.
2.0 OBJECTIVES
At the end of this unit you will have an understanding of the chemical
nature of amino acids, different ways of classifying amino acids and
proteins, formation of peptide bonds and the role of proteins in
biological process.
30
EHS 207 MODULE 2
pH 7 pH 11
31
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Proline Pro P
Serine Ser S
Threonine Thr T
Tryptophan Trp W
Tyrosine Tyr Y
Valine Val V
Note that *Arginine and *Histidine are also grouped as semi essential
amino acids
1.
32
EHS 207 MODULE 2
Glucogenic amino acids are those amino acids in which their carbon
skeleton gets degraded to pyruvate, α ketoglutarate, succinyl CoA,
fumarate and oxaloacetate and then converted to glucose and glycogen.
These include Alanine, Cysteine, Glycine, Arginine, Glutamine,
Isoleucine, and Tyrosine.
These amino acids have the ability to form ketone bodies which is
particularly evident in untreated diabetes mellitus in which large
amounts of ketone bodies are produced by the liver. Degradation of
Leucine which is an exclusively ketogenic amino acid makes a
substantial contribution to the formation of ketone bodies especially
during starvation.
1. Neutral amino acids: These are amino acids that do not contain
any charge on the ‘R’ group. They are further classified into
Aliphatic amino acids which contains a chain of carbon atoms
e.g. Glycine, Alanine, Seine, Threonine, Valine, Leucine,
Isoleucine, Asparagine, Glutamine
Aromatic amino acid which have an aromatic shape or contains
benzene ring e.g. Phenylalanine, Tyrosine, Tryptophan.
Heterocyclic amino acids which have heterocyclic ring i.e. any of
the ring structures which contain different atoms.
Sulphur containing which are amino acids which contain Sulphur
atom e.g. Cysteine and Methionine.
33
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
B. Conjugated Proteins
These yields amino acids and other organic and inorganic
components e.g. Nucleoprotein (a protein
containing Nucleic acids), Lipoprotein (a protein containing
lipids), Phosphoprotein (a protein containing phosphorous),
Metalloprotein (a protein containing metal ions of Fe2+),
Glycoprotein (a protein containing carbohydrates)
A. Fibrous proteins
These proteins are made up of several coiled cross-linked
polypeptide chains. They are insoluble in water and highly
resistant to enzyme digestion. A few sub groups are listed below:
34
EHS 207 MODULE 2
Transport and storage: Many small molecules and ions are transported
by specific proteins e.g. Hb (hemoglobin) transports oxygen in
erythrocytes while myoglobin transports oxygen in muscle. Transferrin
carries iron in the plasma of blood to the liver where it is stored as a
complex with ferritin, another protein.
35
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Mechanical support: The high tensile strength of skin and bone is due
to the presence of collage, a fibrous protein.
4.0 CONCLUSION
5.0 SUMMARY
In this unit you have learnt about the chemical nature of amino acids,
different classification of amino acids and proteins, formation of peptide
bonds and the role of proteins in biological system.
36
EHS 207 MODULE 2
Murray, R. K., Bender, D. A., Botham, K., M., Kennelly, P. J., Rodwell
V.W. and Well, P. A. (2012). Harper’s Illustrated
Biochemistry (29th Edition) McGraw-Hill Medical.
37
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
1.0 Introduction
2.0 Objectives
3.0 Main Content
3.1 Fatty Acids
3.2 Classification of Lipids
3.3 General Functions of Lipids
4.0 Conclusion
5.0 Summary
6.0 Tutor-marked Assignment
7.0 Reference/further reading
1.0 INTRODUCTION
The word lipid was derived from the Greek word lipos meaning fats.
Lipids are heterogeneous group of compounds related either directly or
indirectly to fatty acids. They are insoluble in water but soluble in non-
polar organic solvents such us benzene, chloroform, and ether. They are
present in all living organisms.
2.0 OBJECTIVES
At the end of this unit, you will learn about fatty acids, classification of
lipids and the biological functions of lipids.
1. Saturated fatty acids are the fatty acids without double bonds
i.e. they contain only single bonds along the length of the carbon
chain.
38
EHS 207 MODULE 2
Arachidic acid 20
39
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Triacylglycerols
These are esters of fatty acids with a glycerol and are storage forms of
lipids in mammals. Triacylglycerols also called triacylglycerides exist as
simple or mixed types depending on the type of fatty acids that form
esters with the glycerol.
40
EHS 207 MODULE 2
Steroids
All compounds containing the cyclo-pentano-perhydro-phenanthrene
ring are called steroids. Example of steroids is cholesterol. Cholesterol
is the major sterol in the body. It is a constituent of cell membrane and
provides rigidity to it. It acts as the precursor for all the other steroids in
the body.
Cylo-pentano-perhydro-phenanthrene
Cholesterol
41
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
infertility. So, foods that are rich in essential fatty acids are good for our
health, examples of such foods are fish, poultry products, fruits,
vegetables, nuts (especially walnuts), legumes (especially soya beans),
beef etc. The symptoms of essential fatty acids deficiency are:
i. Growth retardation
ii. Poor wound healing
iii. Dermatitis and hair loss
iv. Kidney and liver diseases
v. Infertility
vi. Depression
4.0 CONCLUSION
Lipids are efficient energy sources for the body and also one of the
structural components of the plasma membrane. Deficiency of essential
fatty acids which are a class of lipid in our body give rise to symptoms
like growth retardation, poor wound healing, dermatitis and hair loss etc.
5.0 SUMMARY
In this unit, you have learnt about fatty acids, classification of lipids and
the symptoms of fatty acid deficiency.
42
EHS 207 MODULE 2
Murray, R. K., Bender, D. A., Botham, K., M., Kennelly, P. J., Rodwell
V.W. and Well, P. A. (2012). Harper’s Illustrated
Biochemistry (29th Edition) McGraw-Hill Medical.
43
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
1.0 Introduction
2.0 Objectives
3.0 Main Content
3.1 Nucleic acids
4.0 Conclusion
5.0 Summary
6.0 Tutor-marked Assignment
7.0 Reference/Further Reading
1.0 INTRODUCTION
Nucleic acids are acidic compounds first discovered in the cell nucleus.
Later they were found in the cytoplasm. They are high molecular weight
nitrogenous organic compounds which play an important role in storage,
transmission and control of all the cellular activities. They are defined as
polynucleotides i.e. chain-like polymers of up to thousands of nucleotide
units. Each nucleotide is a molecular complex of nucleoside and
phosphoric acid.
2.0 OBJECTIVES
On the completion of this unit you will get to understand the chemical
components of nucleic acids, the structure of the DNA and RNA.
The term nucleic acid is the overall name for DNA i.e. deoxyribonucleic
acid and RNA i.e. ribonucleic acid. They are composed of nucleotides,
which are the monomers made of three components: a 5-carbon sugar, a
phosphate group and a nitrogenous base.
Nucleic acids are the most important macromolecules in all living things
because it is the genetic material responsible for the transfer of genetic
information from one generation of organisms to another. The traits we
share with our parents are due to the genes inherited from them. This is
not limited to physical appearance, colour of skin, size of eye balls,
intelligence etc.
44
EHS 207 MODULE 2
1. DNA is made of two helical chains coiled around the same axis,
to form a right-handed double helix.
2. The two chains in the helix are anti-parallel to each other i.e. the
5’-end of the polynucleotide chain and the 3’-end of the other
polynucleotide chain is on the same side and close together.
3. The distance between each turn is 3.6 nm
4. There are 10 nucleotides per turn
5. The spatial relationship between the two strands creates major
and minor grooves between the two strands. In these grooves
some protein interact.
6. The hydrophilic backbones of alternating deoxyribose and
negatively charged phosphate groups are on the outside of the
double bond helix.
7. The hydrophobic pyrimidine and purine bases are inside the
double helix, which stabilizes the double helix of the DNA.
8. The double helix is also stabilized by inter-chain hydrogen bond
formed between a purine and pyrimidine base.
9. A particular purine base, pairs by hydrogen bonds, only with a
particular pyrimidine base i.e. Adenine (A) pairs with Thymine
(T) and Guanine (G) pairs with Cytosine only.
10. Two hydrogen bonds pairs Adenine and Thymine (A = T)
whereas three hydrogen bonds pairs Guanine and Cytosine (G =
C).
11. The base pairs A = T and (G = C) are known as complementary
base pairs.
12. Due to the presence of complementary base pairing, the two
chains of the DNA double helix are complementary to each other.
Hence the number of ‘A’ bases are equal to the number of ‘T’
bases (or ‘G’ is equal to ‘C’) in a given double stranded DNA.
13. One of the strands in the double helix is known as sense strand
i.e. which codes for
45
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
3.6 nm
46
EHS 207 MODULE 2
4.0 CONCLUSION
5.0 SUMMARY
In this unit, you have learnt about the chemical components of nucleic
acid, structure of the DNA and RNA and the differences between them.
47
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Murray, R. K., Bender, D. A., Botham, K., M., Kennelly, P. J., Rodwell
V. W. and Well, P.A. (2012). Harper’s Illustrated
th
Biochemistry (29 edition) McGraw-Hill Medical.
48
EHS 207 MODULE 3
CONTENTS
1.0 Introduction
2.0 Objectives
3.0 Main Content
3.1 Digestion of Carbohydrates
3.2 Absorption of Carbohydrates
3.3 Glycolysis
3.4 Clinical Conditions Associated with Impaired Glycolysis
3.5 Fate of Pyruvate
4.0 Conclusion
5.0 Summary
6.0 Tutor-Marked Assignment
7.0 Reference/Further Reading
1.0 INTRODUCTION
2.0 OBJECTIVES
By the end of this unit, you will be able to:
Liquid food materials like milk, soup, fruit juice escape digestion in
mouth as they are swallowed, but solid foods are masticated thoroughly
before they are swallowed to undergo digestion.
49
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
1. Digestion in Mouth
Digestion of carbohydrates begins in the mouth, where they come in
contact with saliva during mastication. Saliva contains a carbohydrate
splitting enzyme called salivary amylase (ptyalin).
2. Digestion in Intestine
Food from the stomach reaches the duodenum where it meets the
pancreatic juice. The pancreatic juice contains a carbohydrate-splitting
enzyme called pancreatic amylase.
a. Pancreatic amylase
It is also an α – amylase with an optimum pH 7.1. Like salivary ptyalin
pancreatic amylase also requires Cl- for its activity. The enzyme
hydrolyzes α-(1, 4) glycosidic linkage situated in the polysaccharide
molecules thereby liberating free glucose molecules. The pancreatic
amylase acts only on α –1, 4 glycosidic linkages, it cannot act on the α –
1,6 glycosidic linkages which are present at the branching points of
starch and glycogen. These undigested branching points are known as
isomaltose which are digested by an enzyme called isomaltase or α–
dextrinase.
50
EHS 207 MODULE 3
3.3 Glycolysis
51
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Stage 1
Stage 2
Stage 3
Stage 1
1. Phosphorylation of glucose
52
EHS 207 MODULE 3
ATP acts as the phosphate (PO4) donor in the presence of Mg. One high
energy PO4 bond is utilized and ADP is produced. The reaction is
accompanied by considerable loss of free energy as heat.
Note:
Reaction one is irreversible.
One ATP is utilized for phosphorylation of glucose at position 6.
Phosphofructokinase is the key enzyme in glycolysis that regulates the
pathway.
Stage 2
This stage involves the cleavage of fructose 1,6-diphosphate into two
three-carbon fragments which are glyceraldehyde-3-phosphate and a
dihydroxyacetone phosphate catalyzed by aldolase. These resulting three
carbon units are readily interconvertible and are catalyzed by
phosphotriose isomerase.
Note
The reaction is reversible.
There is neither expenditure of energy nor formation ATP.
Stage 3
In this stage, ATP is harvested when the three carbon-fragments are
oxidized to pyruvate. This is an energy-yielding reaction. It consists of
the following reactions:
53
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Significance of glycolysis
1. It is the main route of glucose metabolism.
2. It occurs in all cells of the body.
3. The glycolytic pathway is meant for provision of energy
4. Brain and red blood cells (RBCs) depends only on glucose for
oxidation and production of oxygen
5. In the brain aerobic glycolysis occurs whereas in the RBC, there
is always anaerobic glycolysis due to the absence of the
mitochondria.
6. The initiation of glycolysis is regulated by the ATP concentration
in the cytoplasm.
7. In skeletal muscle, aerobic glycolysis occurs in normal conditions
but during vigorous muscular contraction, anaerobic glycolysis is
the major pathway for energy production as glycolysis provides
ATP. In absence of oxygen, muscles can survive under anaerobic
condition.
Lactic acidosis
It occurs as a result of overproduction of lactate, underutilization of
lactate or inhibition of pyruvate dehydrogenase. It may also be as a
result of rare congenital disorders where the mitochondria do not
function at full capacity or diabetic ketoacidosis as well as liver/kidney
disease. It is characterized by Lactate levels > 5 mm/L and serum pH <
7.35.
54
EHS 207 MODULE 3
4.0 CONCLUSION
55
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
5.0 SUMMARY
In this unit you have learnt about the digestion and absorption of
carbohydrates, reactions of glycolytic pathway and the significance of
the pathway.
Murray, R. K., Bender, D. A., Botham, K., M., Kennelly, P. J., Rodwell
V. W. and Well, P.A. (2012). Harper’s Illustrated
Biochemistry (29th edition) McGraw-Hill Medical.
56
EHS 207 MODULE 3
CONTENTS
1.0 Introduction
2.0 Objectives
3.0 Main Content
3.1 Description of TCA Cycle
3.2 Amphibolic Nature of TCA Cycle
3.3 Anaplerotic Nature of TCA Cycle
3.4 Summary of Oxidative Phosphorylation
4.0 Conclusion
5.0 Summary
6.0 Tutor-Marked Assignment
7.0 References/Further Reading
1.0 INTRODUCTION
The Krebs cycle also known as tricarboxylic cycle or the critic acid
cycle is named after the scientist Sir Hans Krebs (1900-1981) who
discovered it. He proposed the key elements of this pathway in 1937 and
was awarded the Nobel Prize in medicine for the discovery in 1953.
Krebs cycle is a set of continuous reactions (8 steps) occurring in a
cyclic manner in the mitochondrial matrix in eukaryotes and within the
cytoplasm in prokaryotes. Acetyl CoA, the fuel of TCA cycle, enters the
cycle inside the mitochondrial matrix, and gets oxidized to carbon (IV)
oxide (CO2) and H2O while at the same time reducing NAD to NADH
and FAD to FADH2. The NADH and FADH2 can be used by the
electron transport chain to create ATP.
2.0 OBJECTIVES
By the end of this unit, you should understand the TCA cycle,
amphibolic and anaplerotic nature of TCA cycle, oxidative
phosphorylation and inhibitors of the electron transport chain.
57
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Step 1
Condensation: In step 1, the two-carbon compound, acetyl CoA
participates in a condensation reaction with the four-carbon compound,
oxaloacetate to produce citrate, a six-carbon compound catalyzed by
the enzyme citrate synthase. This is the first stable TCA in the cycle
and hence the name TCA cycle.
Step 2
Isomerisation of citrate: Step 2 involves moving the hydroxyl group in
the citrate molecule so that it can later form α-keto acid. This process
involves a sequential dehydration and hydration reaction, to form the D-
isocitrate isomer (with the hydroxyl group now in the desired α-
location), with cis-aconitase as the intermediate. A single enzyme,
aconitase performs this two-step process.
Step 3
Generation of CO2 and NAD+ linked enzyme: Oxidative
decarboxylation takes place in the next reaction. The reaction is
catalyzed by the enzyme isocitrate dehydrogenase. The reaction
involves dehydrogenation to oxalosuccinate, an unstable intermediate
which spontaneously decarboxylates to give α-ketoglutarate. In
addition to decarboxylation, this step produces a reduced nicotinamide
adenine dinucleotide phosphate (NADH) cofactor.
Step 4
A second oxidative decarboxylation step: This step is performed by a
multi-enzyme complex, the α-ketoglutarate dehydrogenation
complex. The multi-step reaction performed by the α-ketoglutarate
dehydrogenation complex is analogous to the pyruvate dehydrogenase
complex, i.e. an α-keto acid undergoes oxidative decarboxylation with
formation of an acetyl CoA i.e. succinyl CoA.
Step 5
Substrate level phosphorylation: Succinyl CoA is a high potential
energy molecule. The energy stored in this molecule is used to form a
high energy phosphate bond in a guanine nucleotide diphosphate (GDP)
molecule. Most of the GTP (Guanine triphosphate) formed is used in the
formation of ATP, by the action of nucleoside diphosphate.
Step 6
Flavin dependent dehydrogenation: The succinate produced by
succinyl CoA-synthetase in the prior reaction needs to be converted to
58
EHS 207 MODULE 3
Step 7
Hydration of a carbon-carbon double bond: Fumarate undergoes a
stereo-specific hydration of the C=C double bond, catalyzed by
fumarate hydratase also known as (fumarase) to produce L-malate.
Step 8
Dehydrogenation reaction that will generate oxaloacetate: L-malate
(malate) is dehydrogenated to produce oxaloacetate by the enzyme
malate dehydrogenase during which one molecule of NAD+ is
converted to NADH + H+. The formation of oxaloacetate completes the
Krebs cycle.
Fig. 3.2: The TCA cycle showing the enzymes and the intermediates
Source: Murray et al. (2012).
59
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
60
EHS 207 MODULE 3
The reduced coenzymes (NADH) and FADH2 from the TCA cycle are
themselves oxidized when they released their protons and electrons. The
electrons are transferred to oxygen, which is the final electron acceptor
through a complex chain of electron-carrying molecules known as the
electron transport chain. During the electron transferring process, large
amount of energy is released and it is conserved in the form of ATP.
This process is called oxidative phosphorylation as shown below.
ADP + Pi ATP
4.0 CONCLUSION
The Krebs cycle is the cycle that takes place in the mitochondrial matrix
of cells and it is responsible for the complete oxidation of acetyl CoA to
carbon (iv) oxide and water.
5.0 SUMMARY
In this unit, you have learnt about the TCA cycle reactions, amphibolic
nature of the TCA cycle, anaplerotic nature of the TCA cycle, oxidative
phosphorylation and inhibitors of the electron transport chain.
61
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Murray, R. K., Bender, D. A., Botham, K., M., Kennelly, P. J., Rodwell
V. W. and Well, P.A. (2012). Harper’s Illustrated
th
Biochemistry (29 edition) McGraw-Hill Medical.
62
EHS 207 MODULE 3
CONTENTS
1.0 Introduction
2.0 Objectives
3.0 Main Content
3.1 Digestion and Absorption of Protein
3.2 Catabolism of Amino Acids
4.0 Conclusion
5.0 Summary
6.0 Tutor-Marked Assignment
7.0 References/Further Reading
1.0 INTRODUCTION
2.0 OBJECTIVES
3. 0 MAIN CONTENT
The entry of proteins into the stomach stimulates the gastric mucosa to
secrete a hormone gastrin which in turn stimulates the secretion of HCl
by the parietal cells of the gastric glands and pepsinogen by the chief
cells.
The HCl thus produced lower the pH of stomach to (pH 1.5 – 2.5) and
acts as an antiseptic killing most of the bacteria and other foreign cells
ingested along with food. The acid also denatures the protein by making
them susceptible to hydrolysis by the action other proteolytic enzymes
called proteases.
active pepsin which cleaves the ingested protein at their amino terminus
of aromatic amino acids (Phe, Tyr, and Trp.) to produce large peptide
fragments and some free amino acids.
Pancreatic Digestion
As the food passes from the stomach to small intestine the low pH of the
food triggers the secretion of the hormone ‘secretin’ into the blood. It
stimulates the pancreas to secrets bicarbonate HCO3 into the small
intestine in order to neutralize HCl. The secretion of HCO3 into the
intestine abruptly raises the pH from 2.5 to 7.0 the entry of amino acids
into the duodenum releases the hormone ‘cholecystokinin’ which
triggers the release of pancreatic juice (that contains many pancreatic
enzymes like trypsinogen, chymotrypsinogen, procarboxypeptidases) by
the exocrine cells of the pancreas. Most of these enzymes are produced
as zymogens (inactive enzymes) by the pancreas in order to protect the
exocrine cells from being digested.
Transamination
Transamination is the transfer of amino group from an amino acid to an
α-keto acid or other amino acids.
64
EHS 207 MODULE 3
65
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
66
EHS 207 MODULE 3
Step 1 CO2 from bicarbonate and NH4 combine together in the liver
mitochondria to form carbamoyl phosphate in presence of ATP and
Mg2+ by the enzyme Carbamoyl phosphate synthetase I (CPSI).
Step 5. Arginine gets cleared off to urea and ornithine by the cytosolic
enzyme arginase. Ornithine is thus re-generated and can be transported
in to the mitochondrion to initiate another round of the urea - cycle.
4.0 CONCLUSION
5.0 SUMMARY
In this unit you have learnt about the digestion and absorption of
proteins and the catabolism of amino acids and the urea cycle.
67
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Discuss:
Murray, R. K., Bender, D. A., Botham, K., M., Kennelly, P. J., Rodwell
V. W. and Well, P.A. (2012). Harper’s Illustrated
th
Biochemistry (29 edition) McGraw-Hill Medical.
68
EHS 207 MODULE 3
CONTENTS
1.0 Introduction
2.0 Objectives
3.0 Main Content
3.1 Digestion and Absorption of Lipids
3.2 β-Oxidation of Fatty Acids
4.0 Conclusion
5.0 Summary
6.0 Tutor-Marked Assignment
7.0 References/Further Reading
1.0 INTRODUCTION
2.0 OBJECTIVE
69
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Digestion of lipids takes place for a longer duration of time. Until and
unless digestion of fats has not taken place, other food materials
(carbohydrates and proteins) cannot be digested because of fats will
cover the food and prevent enzymes reaching the food (hence take a
fatty meal while going on a long journey). The digested lipids enter the
intestinal epithelium by diffusion or by a process called pinocytosis. In
the intestinal wall the free fatty acids and glycerol re-aggregate to form
TAG i.e. here re-synthesis of lipids). These lipids surround a little
amount of protein around them to form chylomicrons which enters into
systemic circulation. The chylomicrons of the circulation move, towards
the adipose tissue, heart, kidney, liver and skeletal muscle. The capillary
walls of these tissues contain an enzyme called lipoprotein lipase which
hydrolyzes the lipids of the chylomicrons and help in their entry into
respective tissue. The lipids are stored as triacylglycerols mainly in the
adipose tissue.
70
EHS 207 MODULE 3
71
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
4.0 CONCLUSION
5.0 SUMMARY
In this unit, you have learnt about been the digestion and absorption of
lipids, metabolism of fatty acids and triacylglycerol and β-oxidation of
fatty acids.
Murray, R. K., Bender, D. A., Botham, K., M., Kennelly, P. J., Rodwell
V. W. and Well, P.A. (2012). Harper’s Illustrated
Biochemistry (29th edition) McGraw-Hill Medical.
72
EHS 207 MODULE 4
CONTENTS
1.0 Introduction
2.0 Objectives
3.0 Main Content
3.1 Water Soluble Vitamins
3.2 Fat Soluble Vitamins
4.0 Conclusion
5.0 Summary
6.0 Tutor-Marked Assignment
7.0 References/Further Reading
1.0 INTRODUCTION
2.0 OBJECTIVES
The water soluble vitamins are the Vitamin B complex and Vitamin C.
Vitamin B and C share few common properties besides their solubility
73
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
The B- Vitamins are essential and must be provided through diet and
they include Thiamine (Vit B1), Riboflavin (Vit B2), Vit B3 Niacin
(Nicotinic acid (or Nicotinamide), Pantothenic acid (Vit B5), Vit B6
(Pyridoxine, pyridoxal, and Pyridoxamine), Vit B9 (Folic Acid), Vit B12
(Cobalamine).
Symptoms
Symptoms include Peripheral neuropathy, exhaustion and anorexia. The
signs may progress to edema and cardiovascular disorders, neurological
and muscular degeneration.
74
EHS 207 MODULE 4
Source: Milk, lean meat, unrefined grains, cereals and from metabolism
of tryptophan.
Required daily allowance (RDA): Adults 17-21 mg, infants 6 mg. The
requirement increases with increased intake of calories, illness, severe
injury, infection, burns, high corn (maize) diet, pregnancy and lactation.
Deficiency
Deficiency leads to failure of growth, loss of weight and anemia.
Pellagra, a disease involving gastrointestinal tract (GIT) and CNS
(central nervous system) also develops.
Symptoms
The disease is characterized by intense irritation and inflammation of the
mucous membranes of the mouth and other parts of the GIT, leading to
gastro- intestinal hemorrhage, dermatitis, dementia and diarrhea. Skin
lesion develops when exposed to sunlight, becomes red, thickened and
scaly. The patient develops gingivitis and stomatitis (tongue gets
swollen)
Vit B6 (Pyridoxine)
This vitamin exists in three forms:Pyridoxine, Pyridoxal and
pyridoxamine and their corresponding phosphates.
RDA: 1.4-2.2 mg for adults, children 0.3-0.4 mg. Patients with anti-
tubercular treatment needs more Vitamin B6.
Deficiency
The deficiency is usually not common, but may result due to intake of
drugs like contraceptives. Alcoholics also suffer from such deficiency.
Oral contraceptives stimulate the synthesis of the enzyme which requires
this vitamin, thus causing deficiency.
75
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Biotin
Biotin is a vitamin and a coenzyme commonly associated with enzymes
performing carboxylation reactions. Biotinis typically linked covalently
to carboxylase enzymes through the α-amino nitrogen of lysine.
Source: Intestinal bacteria, liver, egg, peanuts and milk.
Deficiency
The deficiency is rare since it is found in almost all food stuffs. But
large consumption of raw egg white may lead to deficiency of Biotin.
Avidin, a glycoprotein in egg white binds tightly to biotin and makes it
unavailable for the necessary carboxylation reactions.
Symptoms
Dermatitis, glossitis, Muscle pain, depression, alopecia (loss of hair),
loss of appetite and nausea.
RDA: 3 mg/day.
Deficiency
Deficiency of vitamin B12 causes Anemia (a condition where there is
low level of red blood cells in the body).
76
EHS 207 MODULE 4
RDA: 100 μg/day. (The RDA during lactation and pregnancy is 500 –
800 μg/day)
Deficiency
The causes of folate deficiency are inadequate intake, impaired
absorption, increased demand during pregnancy, lactation and impaired
metabolism that leads to megaloblastic anemia. In this condition
production of erythrocytes slows down, macrocytic erythrocytes with
fragile membrane are formed. Inadequate folate levels during the early
stages of pregnancy increases the risk of neural tube defects (a type of
birth defect) and spontaneous abortions.
Sources: Eggs, liver, animal tissue, whole grain cereals, yeast and
legumes
Deficiency
The deficiency is rare due to its wide distribution however the burning
foot syndrome in prisoners which is associated with reduced capacity for
acetylation is ascribed to pantothenic acid deficiency.
Functions
Vitamin C plays a major role in collagen biosynthesis, degradation of
tyrosine, absorption of iron, formation of steroids
(Steroidogenesis),adrenaline synthesis, bile acid formation, bone mineral
metabolism and acts as potent antioxidant.
77
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
White blood cells (WBC) are rich in vit C and play an important role in
immunity.
Deficiency
Deficiency of vitamin C causes scurvy.
Symptoms
A symptom of extreme vitamin Cdeficiency called scurvy is the
weakening of collagen fibers caused by the failure tohydroxylate proline
and lysine.
Vitamin A
The vitamin is present in the diet as retinol or as β-carotene some of
which is hydrolyzed in the intestine to form retinol. It is a generic term
for a collection of three forms of Vitamins, retinol, retinal and retinoic
acid (Retinoids) all of which are derived from animal and plant sources.
The vitamin is stored mainly in the liver.
Source: A rich source is liver, egg yolk, butter and milk but leafy
vegetables and some fruits provide the largest amount of β-carotene,
Functions
β-carotene plays as an antioxidant role and prevents the development of
diseases like cancer and cardiovascular disease.
Deficiency
Effects on eye
Vitamin A affects growth and differentiation of epithelial cells of the
leading to defective epitheliazation, (a condition affecting the cornea of
the eye). It causes formation of abnormal keratin (keratinization) in the
mucosal cells or cornea of the eye.
Effect on skin
The deficiency causes dryness and roughness of skin developing
keratosis of hair follicles with concomitant deficiency of Vit-B complex.
78
EHS 207 MODULE 4
Sources
Sunlight, Fish oils, egg yolk are naturally rich sources of Vit D.
Functions
i. It promotes bone mineralization.
ii. It promotes absorption of calcium, phosphates.
iii. It enhances the reabsorption of calcium and phosphate by the
kidney.
Deficiency
Deficiency of vitamin D causes rickets (deformation of lower limbs).
Rickets is characterized by the production of soft pliable bones due to
defective mineralization which is secondary to calcium deficiency.
Vitamin E
Vitamin E is required in the human diet but deficiency is rare, except in
pregnancy and the new born, where it is associated with hemolytic
anemia. It exists in the diet as a mixture of eight closely related
compounds called Tocopherols.
Functions
The main function of Vitamin E is that it acts as an antioxidant.
Deficiency
Vitamin E deficiency is a rare but found in complication of prolonged
and severe steatorrhoea, and of prolonged parenteral nutrition.
Deficiency of Vitamin E causes anemia. Generally deficiency is
investigated by measuring plasma (Vitamin E).
79
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Vitamin K
It refers to a group of related compounds, varying the number of
isoprenoid units in its side chain. There are three types, Menaquinone
(K2) present in animals, Phylloquinone (K1) present in plants. Like vit
E, the absorption of Vitamin k is dependent on appropriate fat
absorption.
Functions
It is the only one acting as co-enzyme from the group of Fat soluble
vitamins. This vitamin is also synthesized by intestinal bacteria. It is
required for post translational modifications of several proteins required
in the coagulation cascade
Deficiency
It is widely distributed in nature and produced by the intestinal micro
flora. Virtually ensures that dietary deficiency does not occur in man.
However, it is found in patients suffering from liver diseases
(obstructive jaundice), in new born infants and in patients with
malabsorption. It is associated with bleeding disorders. The placenta is
inefficient at passing maternal Vit K to the fetus and immediately after
birth the circulation concentration drops, but recovers on absorption of
foods. In addition the gut of the new born is sterile, so that the intestinal
micro flora does not provide a source of vit K for several days after
birth. This is the reason why adults who are on prolonged antibiotic
treatment require supplementation of Vit.E.
4.0 CONCLUSION
Vitamins are one of the organic molecules required in the body from
diet for the proper functioning of the body. Some of them act as co-
enzymes that enhances biochemical reactions in the living system while
some act as antioxidants that help prevent the development of diseases.
80
EHS 207 MODULE 4
5.0 SUMMARY
In this unit, you have learnt about the water and fats soluble vitamins
and symptoms of their deficiencies
Murray, R. K., Bender, D. A., Botham, K., M., Kennelly, P. J., Rodwell
V. W. and Well, P.A. (2012). Harper’s Illustrated
th
Biochemistry (29 edition) McGraw-Hill Medical.
81
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
CONTENTS
1.0 Introduction
2.0 Objectives
3.0 Main Content
3.1 Macro and Micro Minerals
3.2 Trace Elements
4.0 Conclusion
5.0 Summary
6.0 Tutor-Marked Assignment
7.0 References /Further Reading
1.0 INTRODUCTION
For any nutrient, there is a range of intake between that which is clearly
inadequate, leading to clinical deficiency disease, and that which is so
much in excess of the body’s metabolic capacity that there may be signs
of toxicity. Between the 2 extremes, there is a level of intake that is
adequate for normal health and the maintenance of metabolic integrity.
Individuals do not have the same requirement for nutrients, even when
calculated on the basis of body size or energy expenditure. Therefore, in
order to assess the adequacy of diets, it is necessary to set a reference
level of intake high enough to ensure that no one either suffers from
deficiency or is at risk of toxicity. Many of the essential minerals are
widely distributed in foods, and most people eating a mixed diet are
likely to receive adequate intakes, although supplements can be used
when some requirements are not adequately met by the diet, or when
chronic or acute deficiencies arise from pathology or injury, etc.
2.0 OBJECTIVES
82
EHS 207 MODULE 4
Dietary Minerals include the macro and micro minerals. Macro minerals
are required in the diet in large amounts (>100 mg/day). They represent
about 80% of body organic matter and include calcium, phosphorus,
potassium, sulfur, sodium, chlorine, and magnesium.
Micro minerals or Trace elements are needed in doses < 100 mg per day.
Important "trace" or minor minerals include iron, cobalt, copper, zinc,
molybdenum, iodine, selenium and cobalt.
Some minerals are necessary for the body, but their exact functions are
unknown. Such include Chromium, Nickel, Bromine, Lithium and
Barium. Non-essential minerals found as contaminants in foodstuffs
include rubidium, silver, gold and bismuth. Toxic minerals include Al,
Pb, Cd and Hg.
Zinc
Total zinc content of the body is about 2g, out of which 60% is in
skeletal muscles and 30% in bones. The highest concentration of Zinc is
seen in Hippocampus area of brain and prostate fluid. More than 300
enzymes are zinc-dependent, including RNA and DNA polymerases,
alkaline phosphatase and carbonic anhydrase. It also forms what is
known as zinc fingers (Zn2+) co-ordinated to four amino acid side
chains), which provide structural stability to many proteins and are
important for protein-protein interactions. These are found in many
signal transduction proteins. Zn is also involved in DNA and protein
synthesis as well as transport of vitamin A, taste perception, wound
healing, Zinc plays a vital role in fertility. In males, it protects the
prostate gland from infection (prostates) and ultimately from
enlargement (prostatic hypertrophy). It also helps maintain sperm count
and mobility and normal levels of serum testosterone. Zinc is important
during pregnancy, for the growing foetus whose cells are rapidly
dividing. Zinc also helps to avoid congenital abnormalities and pre-term
delivery. Zinc is vital in ensuring proper growth and development in
infants, children and teenagers.
83
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Iron
Total body content is 3-5 g, 75% of this is found in blood and the rest in
liver, bone marrow and muscles. Iron is present in almost all cells.
Blood contains 14.5g of Hb per 100 ml. About 75% of total iron is in
hemoglobin, 5% is in myoglobin and 15% in ferritin. Iron carries
oxygen as part of haemoglobin in blood or myoglobin in muscles. It is
required for cellular energy metabolism. Transferrin is the transport
form while Ferritin is the storage form of iron. Transferrin is a
glycoprotein, with a mol wt of 76,500 Daltons. Total iron binding
capacity (TIBC) is a measure of the blood’s capacity to bind iron with
transferring. The ref range is about 400mg/100ml. One third of this
capacity is saturated with iron. Transferrin has a half-life of 7-19 days,
and is a useful index of nutritional status. One molecule of transferrin
can bind two ferric ions. In blood, ceruloplasmin is the ferroxidase,
which oxidizes ferrous to ferric state. Transferrin receptors are present
on most of the body cells, especially on cells which synthesize heme.
The iron-transferrin complex is taken up by the body cells by the
receptor mechanism.
RDA: for men 8 mg, women (19-50 yrs) 18 mg, women > 50 yrs 8 mg.
Sources: Red meat, fish, poultry, eggs, dried fruits, leafy vegetables,
pulses.
Copper
Total body copper is about 100 mg. It is found in muscles, liver, bone
marrow, brain, kidney, heart and hair. It is a required component of
many redox enzymes. Copper containing enzymes are ceruloplasmin,
cytochrome oxidase, tyrosinase, superoxide dismutase and others.
Required for iron absorption and incorporation of iron into hemoglobin.
84
EHS 207 MODULE 4
Sources: Legumes, nuts and seeds, whole grains, organ meats, drinking
water.
RDA: 900 μg
Fluoride
Fluoride is known to prevent caries. In the pits and fissures of premolar
and molar teeth, bacterial fermentation of residual food leads to acid
production. The acid removes enamel and dentine to expose the pulp,
leading to inflammation and toothache. Presence of fluoride will result
in a fluoroapatite layer on the enamel, which protects it from decay. The
safe limit of F is about 1ppm in water (= 1 mg in 1000 ml of water)
Selenium
Selenium (Se) intake depends on the nature of soil in which food crops
are grown. In mammals, glutathione peroxidase is the most important se
containing enzyme. 5”-de-iodinase, which converts thyroxin to T3 also
contains Se. Selenium concentration in testis is the highest in adult
tissue. It is necessary for normal development of spermatozoa. Selenium
also acts as a non specific intracellular anti oxidant, its action being
complementary to that of Vitamin E.
85
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Iodine
Dietary iodine is efficiently absorbed and transported to the thyroid
gland, where it is stored and used for the synthesis of triiodothyronine
and thyroxine. These hormones function in regulating the basal
metabolic rate of adults and the growth and development of children.
Also functions as antioxidant for extrathyroidal organs such as
mammary and salivary glands and for gastric juice production.
4.0 CONCLUSION
Minerals are organic molecules which are required in the body for bone
mineralization and for proper functioning of the body tissues.
5.0 SUMMARY
In this unit, you have been exposed to Macro and Micro minerals.
Murray, R. K., Bender, D. A., Botham, K., M., Kennelly, P. J., Rodwell
V. W. and Well, P.A. (2012). Harper’s Illustrated
th
Biochemistry (29 edition) McGraw-Hill Medical.
86
EHS 207 MODULE 4
UNIT 3 DETOXIFICATION
CONTENTS
1.0 Introduction
2.0 Objectives
3.0 Main Content
3.1 Mechanism of Detoxification
3.2 Detoxification Reactions
3.3 Excretion of Detoxified Xenobiotic
4.0 Conclusion
5.0 Summary
6.0 Tutor Marked Assignment
7.0 References/Further Reading
1.0 INTRODUCTION
87
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
2.0 OBJECTIVE
88
EHS 207 MODULE 4
Phase I
Phase I
Chloral Trichloroethanol
(Chloral is a sedative)
H2 O
H2 O
89
EHS 207 GENERAL BIOCHEMISTRY FOR ENVIRONMENTAL HEALTH
Phase-II
90
EHS 207 MODULE 4
4.0 CONCLUSION
5.0 SUMMARY
1. Define detoxification.
2. Explain the mechanism of detoxification.
3. Write in details with examples reactions involved in oxidation,
reduction, hydrolysis and conjugation.
Murray, R. K., Bender, D. A., Botham, K., M., Kennelly, P. J., Rodwell
V. W. and Well, P.A. (2012). Harper’s Illustrated
Biochemistry (29th edition) McGraw-Hill Medical.
91