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Biochemistry 2
for Dental Students
62BCH 2
Biochemistry BCH 262
This course Prepared by
Dr.Eman Saqr
2
Course Directors
***********
Associate Prof. Dr. Ehab(Male)
Assistant Prof.Dr. Eman Saqr (Female)
Recommended Books, References & Teaching
Materials
•Textbook of biochemistry for dental students by
DM Vasudevan, Sreekumari S and Kannan
Vaidyanathan, 2nd Edition 2011.
•Biochemistry by P.C. Champe, R.A. Harvey and D.R.
Ferrier 3rd Edition 2005 Lippincott’s Illustrated
Reviews
•Handbook of biochemistry (For allied and nursing
students) by Shivananda Nayak B 1st Edition 2007.
Teaching Methodology:
• Lecture. 1hours
•Practical Session. 2 hours
Assessment Tools for each semester:
20% - Mid-Exam
40% - Final Exam
20% - Assignments
20% - Practical
Assignments are:
• 5 marks for each of Research project, Oral, and Quizzes.
• 5 marks for attendance, attitude and participation during
lecture session.
Lectures schedule-Male-Female
Week Date/Saturday Subject Reading assignment Quizzes
1 26/1/2013
Registration
2 2/2/2013
Introduction of
biochemistry and
explain the course
syllabus
Plasma protein
Text book of
Biochemistry for
Dental Students 2th
edition
Chapter 13pp. 122-127
3
9/2/2013 Heme and haemoglobin
metabolism (part 1)
Chapter 15 pp. 137-142
4 16/2/2013
Heme and haemoglobin
metabolism (part 2)
Chapter 15 pp. 142-148 Quiz 1 in the time of
practical session
5
23/2/2013 Connective tissues Chapter 22 pp. 198-201
6 2/3/2013
Fat soluble vitamins Chapter 16 pp. 149-155 Quiz 2 in the time of
practical session
7
9/3/2013 Mid Term Exam
All questions are short notes
8
16/3/2013 Fat soluble vitamins
(continue)
Chapter 16 pp. 149-
155
10 30/3/2013
Water soluble vitamins Chapter 17 pp. 156-
165
11 6/4/2013
Minerals Chapter 18 pp. 167-
176
12
13/4/2013
Biological buffers Chapter 21 pp. 190-
196
Quiz 3 in the time of
practical session
13 20/4/2013
Biochemistry of teeth,
saliva and dental caries
(part 1)
Chapter 8 pp. 67-75
14 27/4/2013
Biochemistry of teeth,
saliva and dental caries
(part 2)
Chapter 8 pp. 67-75 Quiz 4 in the time of
practical session
15 6/5/2013
Control and integration
of metabolism
Chapter 31 pp. 253-
264
16
13/5/2013 Practical Exam
17
20/5/2013 Oral Exam
18
27/5/2013
Final Exam
19 1/6/2013
5/6/2013 Summer Vacation
Research Project
• Each one can choose one from the following hormone as
a subject of the project:
• ACTH, ADH, FSH, LH, TSH, PTH, Glucagon, Calcitonin,
GnRH, TRH, ANF, Estrogens, Progesterone, Androgens,
Catechol amines, Insulin, Glucocorticoids, Acetyl
choline.
• Dead line to record names of each one with his/her
subject on Wednesday, 13/2/2013.
• Five students from each group will discuss their project
weekly starting from the third week according to their
presence in the attendance sheet.
• The only excuse is by recommended medical certificate.
For FemaleTime Table
Group One Group Two Group Three
Theoretical
Wednesday Wednesday Wednesday
11-12 12-1 1-2
Class 12 Class 12 Class 12
Practical
Monday Monday Monday
12-2 8-10 10-12
Office Hours Saturday 12-2
For MaleTime Table
Group One Group Two Group Three
Theoretical
Wednesday Wednesday Wednesday
5-6 5-6 5-6
Audio-3 Audio-3 Audio-3
Practical
Monday Monday Monday
8-10 4-6 6-8
Office Hours Saturday 6-8
Blood Biochemistry
Plasma proteins,
Immunoglobulin and
Hemoglobin
Blood
• Total blood volume is about 4.5 to 5 liters in adult human being.
• Blood is a highly specialized tissue composed of more than 4,000
different kinds of components. Four of the most important ones are
red cells, white cells, platelets, and plasma.
• Normally, 55% of our blood's volume is made up of plasma.
• Plasma also contains blood clotting factors, sugars, lipids, vitamins,
minerals, hormones, enzymes, antibodies, and other proteins.
• It is likely that plasma contains some of every protein produced by
the body--approximately 500 have been identified in human plasma
so far.
• The de-fibrinated plasma is called serum, which lacks coagulation
factors including prothrombin and fibrinogen.
Plasma Proteins
• Total protein content of normal plasma is 6 to 8
g/100 ml.
• The plasma proteins consist of:
 Albumin (3.5 - 5 g/dl).
 Globulins (2.5 – 3.5 g/dl).
 Fibrinogen (200 – 400 mg/dl).
• The albumin : globulin ratio is usually between 1.2 :
1 to 1.5 : 1.
• Almost all plasma proteins, except immunoglobulin
are synthesized in liver.
Electrophoresis
• In clinical laboratory, electrophoresis
is employed regularly for separation
of serum proteins.
• The term electrophoresis refers to
the movement of charged particles
through an electrolyte when
subjected to an electric field
Normal value and Interpretations
• In agar gel electrophoresis, normal
serum is separated into five bands,
Albumin, Alpha-1-globulin, Alpha-2-
globulin, Beta-globulin and Gamma
globulin.
Albumin has the maximum and gamma
globulin has the minimum mobility in
the electrical field.
Abnormal Patterns in Clinical Diseases
• Various abnormalities can identified
in the electrophoretic pattern.
Chronic infections:
The gamma globulins are increased,
but the increase is smooth and wide
based.
Transport proteins
Blood is a watery medium; so lipids and lipid
soluble substances will not easily mix in the
blood. Hence, such molecules are carried by
specific carrier proteins.
1. Albumin: It is an important transport protein,
which carries bilirubin, free fatty acids,
calcium and drug.
2. Pre-albumin or transthyretin: It carries
thyroid hormones, thyroxin (T4) and tri-iodo
thyronine (T3). Its half life in plasma is only 1
day.
3. Thyroxine binding globulin (TBG): It is the
specific carrier molecule for thyroxine and tri-
iodo thyronine. TBG level is increased in
pregnancy; but decreased in nephrotic
syndrome.
4. Retinol binding protein (RBP): It carries
vitamin A.
5- Transcortin or cortisol binding globulin
(CBG): Transports cortisol and corticosterone.
6. Transferrin: It carries iron in plasma.
Acute Phase Proteins
• The level of certain proteins in blood may
increase 50 to 1000 folds in various
inflammatory and neoplastic conditions.
• Such proteins are acute phase proteins.
• Important acute phase proteins are:
1. C-Reactive Protein (CRP).
2. Ceruloplasmin.
1. C-Reactive Protein (CRP):
• It is thus named because it reacts with C-
polysaccharide of capsule of
pneumococci.
• It is synthesized in liver.
• It can stimulate macrophage
phagocytosis.
• When the inflammation has subsided,
CRP quickly falls, followed later by ESR
(erythrocyte sedimentation rate).
2. Ceruloplasmin:
I. Ceruloplasmin is blue in colour.
II. It is synthesized in liver. It contains 6 to 8 copper
atoms per molecule.
III. Ceruloplasmin is also called Ferroxidase, an
enzyme which helps in the incorporation of iron
into transferrin.
IV. Ceruloplasmin is an acute phase protein. So its
level in blood may be increased in all
inflammatory conditions, collagen disorders and in
malignancies.
Albumin
Function of Albumin
1. Colloid osmotic pressure of plasma
• Protein cannot easily escape out of blood vessels,
and therefore, proteins exert the ‘effective osmotic
pressure’ (EOP).
• The maintenance of blood volume is dependent on
EOP.
• If protein concentration reduced, so EOP will
reduced, then return of water into blood vessel is
diminished. Leading to accumulation of water in
tissues, this called edema.
2. Transport Function
Albumin is the carrier of various hydrophobic
substances in the blood. Being a watery medium,
blood cannot solubilize lipid components and
lipophilic compounds such as:
I. Bilirubin and nonesterified fatty acids are
specifically transported by albumin.
II. Drugs (sulpha, aspirin, salicylates, dicoumarol,
phenytoin).
III. Hormones: Steroid hormones, thyroxine.
IV. Metals: Calcium, copper and heavy metals are
nonspecifically carried by albumin.
3. Nutritional function
• All tissue cells can take up albumin by
pinocytosis.
• It is then broken down to amino acid
level.
• So albumin may be considered as the
transport form of essential amino
acids from liver to other tissues.
Edema
Hypoalbuminemia will result in tissue edema.
I. Malnutrition, where albumin synthesis is
depressed (generalized edema).
II. Nephrotic syndrome, where albumin is lost
through urine (facial edema). Presence of albumin
in urine is called albuminuria.
III. Cirrhosis of liver (mainly ascites). Albumin
synthesis is decreased.
IV. Chronic congestive cardiac failure, venous
congestion will cause increased hydrostatic
pressure and decreased return of water into
capillaries and so pitting edema of feet may result.
Albumin-Globulin Ratio
• In hypoalbuminemia, there will be a
compensatory increase in globulins
which are synthesized by the
reticuloendothelial system.
• Albumin-globulin ratio (A/G ratio) is
thus altered or even reversed. This
again leads to edema.
Immunoglobulins
• Immunoglobulin is abbreviated as Ig.
• The terms gamma globulin and immunoglobulin are
not synonymous.
• Gamma globulin is the term describing its mobility
in electrical field.
• Most of the immunoglobulins have the gamma
mobility; but some may move along with beta or
even with alpha globulins.
• Immunoglbulin is a functional term, while gamma
globulin is a physical term.
Heavy and light chains
• Immunoglobulin consists of light chain (less number
of amino acid) and heavy chain (large number of
amino acid).
• According to heavy chain immunoglobulin
differentiated to 5 major classes:
1. IgG is made up of heavy chain ɣ (gamma).
2. IgM has μ (mu) heavy chain.
3. IgA has α (alpha) heavy chain.
4. IgD contains δ (delta) chain.
5. IgE heavy chain called ε (epsilon).
• The light chain either ҡ (kappa) or λ (lambda).
Different classes of Immunoglobulins
1. Immunoglobulin G (IgG)
• IgG contains 2 heavy chains(composed of 440
amino acids) and 2 light chains (composed of 214
amino acids) combined through disulphide bridges.
• It is the antibody seen in secondary immune
response.
• It can pass from vascular compartment to
interstitial space.
• It can cross placental barrier, and protects the new
born child from infections.
2. Immunoglobulin M (IgM)
• Ig M are macroglobulins.
• Five subunits, each having 4 peptide chains (total 10
heavy chains and 10 light chains) are joined
together by a J-chain polypeptide.
• It can combined with 5 antigen simultaneously, and
so IgM is very effective for agglutinating bacteria.
• Being a large molecule, it cannot come out of
vascular space.
• IgM are the predominant class of antibodies in
primary response.
Immunoglobulin M (IgM)
3. Immunoglobulin A (IgA)
• IgA usually are dimers (total 4 heavy chains
and 4 light chains). The J-chain connects the
dimers.
• They are secretory antibodies seen in
seromucous secretions of gastrointestinal
tract, nasopharyngeal tract, urogenital tract,
tears, saliva, sweats, etc.
• The dimers are stabilized against proteolytic
enzymes by the secretory piece.
4. Immunoglobulin E (IgE)
• They mediate allergy, hypersensitivity and anaphylaxis.
• They have the property to fix on mast cells and
basophils. When certain antigens such as penicillin are
injected a few times, IgE class antibodies are produced
which anchor on mast cells.
• When the same antigen is injected next time, the
antigen fixes on cell surface antibodies, causing mast cell
degranulation, and release of histamine and slow
reacting substance.
• This leads to vasodilatation, hypotension and
bronchiolar constriction.
• This is the basis of penicillin anaphylaxis, hay fever
caused by fungus, asthma by pollen and urticaria by
absorbed food elements.

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  • 1. Biochemistry 2 for Dental Students 62BCH 2
  • 2. Biochemistry BCH 262 This course Prepared by Dr.Eman Saqr 2 Course Directors *********** Associate Prof. Dr. Ehab(Male) Assistant Prof.Dr. Eman Saqr (Female)
  • 3. Recommended Books, References & Teaching Materials •Textbook of biochemistry for dental students by DM Vasudevan, Sreekumari S and Kannan Vaidyanathan, 2nd Edition 2011. •Biochemistry by P.C. Champe, R.A. Harvey and D.R. Ferrier 3rd Edition 2005 Lippincott’s Illustrated Reviews •Handbook of biochemistry (For allied and nursing students) by Shivananda Nayak B 1st Edition 2007.
  • 4. Teaching Methodology: • Lecture. 1hours •Practical Session. 2 hours Assessment Tools for each semester: 20% - Mid-Exam 40% - Final Exam 20% - Assignments 20% - Practical Assignments are: • 5 marks for each of Research project, Oral, and Quizzes. • 5 marks for attendance, attitude and participation during lecture session.
  • 5. Lectures schedule-Male-Female Week Date/Saturday Subject Reading assignment Quizzes 1 26/1/2013 Registration 2 2/2/2013 Introduction of biochemistry and explain the course syllabus Plasma protein Text book of Biochemistry for Dental Students 2th edition Chapter 13pp. 122-127 3 9/2/2013 Heme and haemoglobin metabolism (part 1) Chapter 15 pp. 137-142 4 16/2/2013 Heme and haemoglobin metabolism (part 2) Chapter 15 pp. 142-148 Quiz 1 in the time of practical session 5 23/2/2013 Connective tissues Chapter 22 pp. 198-201 6 2/3/2013 Fat soluble vitamins Chapter 16 pp. 149-155 Quiz 2 in the time of practical session 7 9/3/2013 Mid Term Exam All questions are short notes 8 16/3/2013 Fat soluble vitamins (continue) Chapter 16 pp. 149- 155
  • 6. 10 30/3/2013 Water soluble vitamins Chapter 17 pp. 156- 165 11 6/4/2013 Minerals Chapter 18 pp. 167- 176 12 13/4/2013 Biological buffers Chapter 21 pp. 190- 196 Quiz 3 in the time of practical session 13 20/4/2013 Biochemistry of teeth, saliva and dental caries (part 1) Chapter 8 pp. 67-75 14 27/4/2013 Biochemistry of teeth, saliva and dental caries (part 2) Chapter 8 pp. 67-75 Quiz 4 in the time of practical session 15 6/5/2013 Control and integration of metabolism Chapter 31 pp. 253- 264 16 13/5/2013 Practical Exam 17 20/5/2013 Oral Exam 18 27/5/2013 Final Exam 19 1/6/2013 5/6/2013 Summer Vacation
  • 7. Research Project • Each one can choose one from the following hormone as a subject of the project: • ACTH, ADH, FSH, LH, TSH, PTH, Glucagon, Calcitonin, GnRH, TRH, ANF, Estrogens, Progesterone, Androgens, Catechol amines, Insulin, Glucocorticoids, Acetyl choline. • Dead line to record names of each one with his/her subject on Wednesday, 13/2/2013. • Five students from each group will discuss their project weekly starting from the third week according to their presence in the attendance sheet. • The only excuse is by recommended medical certificate.
  • 8. For FemaleTime Table Group One Group Two Group Three Theoretical Wednesday Wednesday Wednesday 11-12 12-1 1-2 Class 12 Class 12 Class 12 Practical Monday Monday Monday 12-2 8-10 10-12 Office Hours Saturday 12-2
  • 9. For MaleTime Table Group One Group Two Group Three Theoretical Wednesday Wednesday Wednesday 5-6 5-6 5-6 Audio-3 Audio-3 Audio-3 Practical Monday Monday Monday 8-10 4-6 6-8 Office Hours Saturday 6-8
  • 11. Blood • Total blood volume is about 4.5 to 5 liters in adult human being. • Blood is a highly specialized tissue composed of more than 4,000 different kinds of components. Four of the most important ones are red cells, white cells, platelets, and plasma. • Normally, 55% of our blood's volume is made up of plasma. • Plasma also contains blood clotting factors, sugars, lipids, vitamins, minerals, hormones, enzymes, antibodies, and other proteins. • It is likely that plasma contains some of every protein produced by the body--approximately 500 have been identified in human plasma so far. • The de-fibrinated plasma is called serum, which lacks coagulation factors including prothrombin and fibrinogen.
  • 12. Plasma Proteins • Total protein content of normal plasma is 6 to 8 g/100 ml. • The plasma proteins consist of:  Albumin (3.5 - 5 g/dl).  Globulins (2.5 – 3.5 g/dl).  Fibrinogen (200 – 400 mg/dl). • The albumin : globulin ratio is usually between 1.2 : 1 to 1.5 : 1. • Almost all plasma proteins, except immunoglobulin are synthesized in liver.
  • 13. Electrophoresis • In clinical laboratory, electrophoresis is employed regularly for separation of serum proteins. • The term electrophoresis refers to the movement of charged particles through an electrolyte when subjected to an electric field
  • 14.
  • 15. Normal value and Interpretations • In agar gel electrophoresis, normal serum is separated into five bands, Albumin, Alpha-1-globulin, Alpha-2- globulin, Beta-globulin and Gamma globulin. Albumin has the maximum and gamma globulin has the minimum mobility in the electrical field.
  • 16. Abnormal Patterns in Clinical Diseases • Various abnormalities can identified in the electrophoretic pattern. Chronic infections: The gamma globulins are increased, but the increase is smooth and wide based.
  • 17. Transport proteins Blood is a watery medium; so lipids and lipid soluble substances will not easily mix in the blood. Hence, such molecules are carried by specific carrier proteins. 1. Albumin: It is an important transport protein, which carries bilirubin, free fatty acids, calcium and drug. 2. Pre-albumin or transthyretin: It carries thyroid hormones, thyroxin (T4) and tri-iodo thyronine (T3). Its half life in plasma is only 1 day.
  • 18. 3. Thyroxine binding globulin (TBG): It is the specific carrier molecule for thyroxine and tri- iodo thyronine. TBG level is increased in pregnancy; but decreased in nephrotic syndrome. 4. Retinol binding protein (RBP): It carries vitamin A. 5- Transcortin or cortisol binding globulin (CBG): Transports cortisol and corticosterone. 6. Transferrin: It carries iron in plasma.
  • 19. Acute Phase Proteins • The level of certain proteins in blood may increase 50 to 1000 folds in various inflammatory and neoplastic conditions. • Such proteins are acute phase proteins. • Important acute phase proteins are: 1. C-Reactive Protein (CRP). 2. Ceruloplasmin.
  • 20. 1. C-Reactive Protein (CRP): • It is thus named because it reacts with C- polysaccharide of capsule of pneumococci. • It is synthesized in liver. • It can stimulate macrophage phagocytosis. • When the inflammation has subsided, CRP quickly falls, followed later by ESR (erythrocyte sedimentation rate).
  • 21. 2. Ceruloplasmin: I. Ceruloplasmin is blue in colour. II. It is synthesized in liver. It contains 6 to 8 copper atoms per molecule. III. Ceruloplasmin is also called Ferroxidase, an enzyme which helps in the incorporation of iron into transferrin. IV. Ceruloplasmin is an acute phase protein. So its level in blood may be increased in all inflammatory conditions, collagen disorders and in malignancies.
  • 22. Albumin Function of Albumin 1. Colloid osmotic pressure of plasma • Protein cannot easily escape out of blood vessels, and therefore, proteins exert the ‘effective osmotic pressure’ (EOP). • The maintenance of blood volume is dependent on EOP. • If protein concentration reduced, so EOP will reduced, then return of water into blood vessel is diminished. Leading to accumulation of water in tissues, this called edema.
  • 23. 2. Transport Function Albumin is the carrier of various hydrophobic substances in the blood. Being a watery medium, blood cannot solubilize lipid components and lipophilic compounds such as: I. Bilirubin and nonesterified fatty acids are specifically transported by albumin. II. Drugs (sulpha, aspirin, salicylates, dicoumarol, phenytoin). III. Hormones: Steroid hormones, thyroxine. IV. Metals: Calcium, copper and heavy metals are nonspecifically carried by albumin.
  • 24. 3. Nutritional function • All tissue cells can take up albumin by pinocytosis. • It is then broken down to amino acid level. • So albumin may be considered as the transport form of essential amino acids from liver to other tissues.
  • 25. Edema Hypoalbuminemia will result in tissue edema. I. Malnutrition, where albumin synthesis is depressed (generalized edema). II. Nephrotic syndrome, where albumin is lost through urine (facial edema). Presence of albumin in urine is called albuminuria. III. Cirrhosis of liver (mainly ascites). Albumin synthesis is decreased. IV. Chronic congestive cardiac failure, venous congestion will cause increased hydrostatic pressure and decreased return of water into capillaries and so pitting edema of feet may result.
  • 26. Albumin-Globulin Ratio • In hypoalbuminemia, there will be a compensatory increase in globulins which are synthesized by the reticuloendothelial system. • Albumin-globulin ratio (A/G ratio) is thus altered or even reversed. This again leads to edema.
  • 27. Immunoglobulins • Immunoglobulin is abbreviated as Ig. • The terms gamma globulin and immunoglobulin are not synonymous. • Gamma globulin is the term describing its mobility in electrical field. • Most of the immunoglobulins have the gamma mobility; but some may move along with beta or even with alpha globulins. • Immunoglbulin is a functional term, while gamma globulin is a physical term.
  • 28. Heavy and light chains • Immunoglobulin consists of light chain (less number of amino acid) and heavy chain (large number of amino acid). • According to heavy chain immunoglobulin differentiated to 5 major classes: 1. IgG is made up of heavy chain ɣ (gamma). 2. IgM has μ (mu) heavy chain. 3. IgA has α (alpha) heavy chain. 4. IgD contains δ (delta) chain. 5. IgE heavy chain called ε (epsilon). • The light chain either ҡ (kappa) or λ (lambda).
  • 29. Different classes of Immunoglobulins 1. Immunoglobulin G (IgG) • IgG contains 2 heavy chains(composed of 440 amino acids) and 2 light chains (composed of 214 amino acids) combined through disulphide bridges. • It is the antibody seen in secondary immune response. • It can pass from vascular compartment to interstitial space. • It can cross placental barrier, and protects the new born child from infections.
  • 30.
  • 31. 2. Immunoglobulin M (IgM) • Ig M are macroglobulins. • Five subunits, each having 4 peptide chains (total 10 heavy chains and 10 light chains) are joined together by a J-chain polypeptide. • It can combined with 5 antigen simultaneously, and so IgM is very effective for agglutinating bacteria. • Being a large molecule, it cannot come out of vascular space. • IgM are the predominant class of antibodies in primary response.
  • 33. 3. Immunoglobulin A (IgA) • IgA usually are dimers (total 4 heavy chains and 4 light chains). The J-chain connects the dimers. • They are secretory antibodies seen in seromucous secretions of gastrointestinal tract, nasopharyngeal tract, urogenital tract, tears, saliva, sweats, etc. • The dimers are stabilized against proteolytic enzymes by the secretory piece.
  • 34. 4. Immunoglobulin E (IgE) • They mediate allergy, hypersensitivity and anaphylaxis. • They have the property to fix on mast cells and basophils. When certain antigens such as penicillin are injected a few times, IgE class antibodies are produced which anchor on mast cells. • When the same antigen is injected next time, the antigen fixes on cell surface antibodies, causing mast cell degranulation, and release of histamine and slow reacting substance. • This leads to vasodilatation, hypotension and bronchiolar constriction. • This is the basis of penicillin anaphylaxis, hay fever caused by fungus, asthma by pollen and urticaria by absorbed food elements.