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3- TRICARBOXYLIC ACID (TCA) CYCLE
4- Metabolism of carbohydrates
6- Insulin and diabetes mellitus
9. METABOLISM OF PURINE AND PYRIMIDINE NUCLEOTIDES
10. BIOCHEMICAL CHANGES IN LARGE INTESTINE
11. METABOLISM OF XENOBIOTICS (DETOXIFICATION)
1.1. Nature of enzymes, enzyme terminology and mechanism of enzyme action [lock and key model (Fisher hypothesis) and induced fit model (Koshland hypothesis)].
1.2. Types of enzymes catalyzed reactions (exergonic reactions (exothermic), endergonic reactions (endothermic) and isothermic reactions).
1.3. Enzyme Specificity (absolute specificity, optical specificity (stereochemical specificity) and group specificity).
1.4. Isoenzymes (Isozymes): Lactate dehydrogenase and creatine kinase
1.6. Factors Affecting the Rate of Enzyme Action
1- Temperature 2- pH 3- Substrate concentration (Michaelis-Menten equation and Lineweaver -Burk plot),4- Enzyme concentration, 5-Time, 6- Reaction products and 7- Cofactors
1.7. Enzyme activation: Activation of zymogens, activation by metal ions, allosteric activation and covalent modification.
1.8. Enzyme inhibitors: Nonspecific inhibitors, specific inhibitors (competitive and noncompetitive).
1.9. Regulation of enzyme activity: Changing the absolute amount of the enzyme present, changing the catalytic activity of the enzyme and compartmentation of enzymes.
1.10.Classification of Enzymes
1.10.1. Oxidoreductases: dehydrogenases, oxidases, hydroproxidases and oxygenases
1.10.2.Transferases: phosphotransferases, aminotransferases and methyktransferases.
1.10.3.Hydrolases: glycosidases, peptidases, esterases and phosphatases.
1.10.4.Phosphorylases.
1.10.5.Lyases: dehydratases, decarboxylases, ammonia lyase, aldolase and desulfhydrases.
1.10.6.Ligases: synthetases and synthases.
1.10.7.Isomerases: epimerases, aldose-ketose isomerases, cis-trans isomerases and mutases
By the end of this course the student should be able to describe the nature of enzymes and the process of enzyme catalysis as the basis of biochemical transformation of cellular substances. He should understand the mechanism of enzyme action and its importance in deducing the structure of metabolic antagonists. He should also understand the different classes of enzymes, how do they function and how are they helped by coenzymes and metal ion activators. He should be able to describe the location of enzymes within cells and their organelles. He should be able to explain the relationship among enzymes, their -physiologic and metabolic function, and how function is controlled. He should be able to show how enzymes work in sequence to form a metabolic pathway which is subject to various types of control. He should be able to understand how quantitative assays of selected enzyme activities in the blood and other body fluids help to diagnose disease.
2.1. Anabolism and catabolism (three stage of catabolism).
2.2. ATP - ADP Cycle, low and high Energy Bonds
2.3. Electron transport chain: Components of ETC, ATP synthesis (chemiosmotic theory), ATP synthase, ATP - ADP translocator (transporter), control of oxidation in ETC, inhibitors of ETC, uncouplers and sources of NADH and FADH2 for ETC.
2.4. Oxidation of extra-mitochondrial NADH: glycerol phosphate shuttle and malate shuttle
2.5. Oxidative phosphorylation: Respiratory chain level oxidative phosphorylation and substrate level oxidative phosphorylation
The student should be able to grasp properly how do cells get energy from the oxidation of foodstuffs. He should be able to predict direction of a reaction from changes in free energy and to explain how the energy from one reaction promotes a second reaction. He should also be able to demonstrate how oxidative phosphorylation produces high energy bonds and to explain how oxidation of metabolites of carbohydrates, fats and proteins produce energy.
3- TRICARBOXYLIC ACID (TCA) CYCLE
3.1. Site and Steps
3.2. Importance of citric acid cycle: Catabolic functions and energy production and importance of TCA cycle intermediates
3.3. Regulation of enzymes of citric acid cycle
The student should be able to illustrate that mitochondria control and regulate metabolic pathways. The steps of the TCA cycle and its biochemical significance should be clearly grasped. The correlation between the TCA cycle, ETC and other metabolic pathways is demonstrated.
4- Metabolism of carbohydrates
4.1. Dietary carbohydrates
4.2. Digestion of carbohydrates, inherited lactase deficiency (lactose Intolerance) and inherited sucrase deficiency
4.3. Absorption of monosaccharides: Simple diffusion, facilitated transport and cotransport (active transport) and inhibitors of glucose absorption
Fate of Absorbed Sugars
4.4. Glucose uptake by tissues: GLUT-1, GLUT-2, GLUT-3, GLUT-4, GLUT-5 and SGLT-1, effect of insulin transporters.
4.5. Glycolysis (Embden – Meyerhof Pathway): Site and steps, importance, energy production during aerobic and anaerobic conditions, importance of glycolytic intermediates, importance of glycolysis in red cells (Rapoport - Luebering cycle and hemolytic anemia due to deficiency of glycolytic enzymes), regulation of glycolysis (regulation of individual key enzymes, role of phosphofructokinase-2, substrate activation, product feedback inhibition and hormonal regulation), inhibitors of glycolysis and Cori cycle.
4.6. Metabolism of pyruvate: Sources and fate, conversion of pyruvate to active acetate, regulation of the activity of pyruvate dehydrogenase complex, conversion of pyruvate to oxaloacetate.
4.7. Summary for complete oxidation of glucose
4.8. Hexose monophosphate pathway (hexose pentose pathway): Site and steps, oxidative phase and non-oxidative phase, importance of pentose phosphate pathway in different tissuea and in red cells (favism) and regulation of HMP.
4.9. Uronic acid pathway: Site and steps, importance and essential pentosuria.
4.10. Glycogenesis: Glycogen synthase and branching enzyme and regulation of activity of glycogen synthase.
4.11. Glycogenolysis: Glycogen phosphorylase, Debranching enzyme. regulation of activity of glycogen phosphorylase, muscle phosphorylase and glycogen storage diseases (glycogenosis).
4.12. Gluconeogenesis: Site and steps, ATP and NADH which are utilized for gluconeogenesis, gluconeogenic substrates, importance of gluconeogenesis, regulation of gluconeogenesis (effect of increased fatty acid oxidation on gluconeogenesis, role of PFK-2 / F-2,6-BPase and hormonal regulation) and fructose - 1,6 - bisphosphatase deficiency.
4.13. Fructose metabolism: Utilization of fructose in liver and in extrahepatic tissues, synthesis of free fructose in seminal vesicles, essential fructosuria and hereditary fructose intolerance.
4.14. Galactose metabolism: Utilization in liver, synthesis of lactose and galactose containing compounds and galactosemia.
4.15. Metabolism of aminosugars: Synthesis of aminosugares and mucopolysaccharidoses.
4.16. Blood glucose: Blood glucose levels, sources of blood glucose and regulation of blood glucose (regulation by different tissues and organs and by hormones: insulin and anti-insulin hormones).
4.17. Abnormalities of Blood Glucose: Hypoglycemia and diabetes mellitus (explained later on)
4.18. Hypoglycemia: Postprandial hypoglycemia and fasting hypoglycemia
4.19. Glycosuria: glucosuria, fructosuria, galactosuria, pentosuria and lactosuria.
By the end of this course the student should be able, to know what are the major dietary carbohydrates, how are they digested and absorbed and how may defects in these processes lead to disease. He should understand how is glucose oxidized to liberate energy and how is this process properly regulated according to the body requirement. He should be able to relate carbohydrate metabolism to the functioning of the Krebs’ cycle. He should also know the importance of the alternative pathways for glucose oxidation and how may defects in these pathways lead to disease.
He should understand how may glucose be stored in the form of glycogen and how may it be produced by glycogenolysis, as well as the enzyme defects which may occur in these processes. He should also know the relative importance of glycogenolysis and gluconeogenesis in maintaining the blood sugar level during fasting and how are these processes regulated. The student should appreciate the importance of the defects in the oxidation of galactose and fructose. The role of different organs and hormones in the regulation of the blood glucose level and the causes of hyperglycemia, hypoglycemia and glycosuria should be appreciated.
5.1. Importance of dietary lipids
5.2. Digestion of lipids: Digestion of triacylglycerols (TAG), phospholipids and cholesteryl esters.
5.3. Absorption of lipids: Formation of micelles, chylomicron formation, steatorrhea and chyluria.
5.4. Fate of absorbed lipids
5.5. Depot fat metabolism: Lipogenesis or synthesis of triacylglycerols (TAG) and lipolysis (hormone sensitive lipase).
5.6. Metabolism of fatty acids
5.6.1. Oxidation of saturated fatty acids: b-oxidation of fatty acids (site and steps, energy production regulation, oxidation of odd-chain fatty acids and metabolic disorders of fatty acid oxidation), a -oxidation of fatty acids (Refsum's disease) and w- Oxidation of fatty acids.
5.6.2. Synthesis of saturated fatty acids: The cytosolic system for de novo synthesis of fatty acids (Fatty acid synthase multienzyme complex) and microsomal system for chain elongation, and regulation of fatty acid synthesis.
5.6.3. Oxidation and synthesis of USFA
5.7. Metabolism of eicosanoids: Synthesis (cyclooxygenase & lipoxygenase pathways) and functions of eicosanoids,
5.8. Metabolism of conjugated lipids: Metabolism of phosphoglycerides and sphingolipids.
5.9. Metabolism of cholesterol: Dietary sources, biosynthesis, functions and excretion of cholesterol. -Plasma cholesterol (LDL/HDL cholesterol), hypercholesterolemia and hypocholesterolemia.
5.10. Metabolism of ketone bodies: Ketogenesis, ketolysis and ketosis (causes of ketosis, changes in different tissues, ketogenic substances, anti-ketogenic substances and complication of ketosis).
5.11. Blood lipids: Types of plasma lipids, types and composition of plasma lipoproteins, separation of plasma lipoproteins (electrophoresis and ultracentrifugation fractions), metabolism of different lipoproteins, disorders of plasma lipoproteins (dyslipoproteinemias)
5.12. Role of liver in lipid metabolism, lipotropic factors and fatty liver.
By the end of this course the student should be able to know what are the major dietary lipids, how are they digested and absorbed, and how may defects in these processes lead to disease. He should understand what happens to fats after absorption. He should appreciate the difference between depot and tissue fat and the regulation of the breakdown of the former under different dietary conditions. The student should understand how are fatty acids oxidized and the relation of this to the formation and breakdown of ketone bodies. He should also understand how are fatty acids built up and the regulation of this process under different dietary conditions.
The student should also understand the biosynthesis of phospholipids and glycolipids and how may deficient synthesis affect their functions.
The student should grasp well the metabolism of the unsaturated fatty acids and their importance in the formation of the prostaglandins, thromboxanes and leucotrienes.
He should also be able to appreciate the relation between the metabolism of cholesterol and the plasma lipoproteins and the development of the different types of hyper and hypolipoproteinemias together with the relationship of this to the development of atherosclerosis.
The role of liver in lipid metabolism and its relation to the causation of fatty liver should be clearly appreciated by the student.
6- Insulin and diabetes mellitus
6.1. Insulin: chemistry of insulin, synthesis, storage, secretion, catabolism and mechanism of Insulin action. Effects of insulin on glucose, lipid and protein metabolism.
6.2. Diabetes mellitus (DM): Primary types of DM [type-1 (insulin dependent diabetes mellitus or IDDM) and type-2 (non-insulin dependent diabetes mellitus or NIDDM)]. Metabolic changes in diabetes mellitus (changes in carbohydrate, lipid and protein metabolism, other changes, vascular complications, diabetic cataract, retinopathy, nephropathy and neuropathy).
6.3. Tests for diagnosis and follow up of diabetes mellitus: Measurement of blood glucose (plasma glucose), oral glucose tolerance test (OGTT) and measurement of glycosylated - Hb (HbA1c).
6.4. Diabetic Coma: Hyperglycemic and hypoglycemic coma.
By the end of this course the student should understand diabetes mellitus, its causes, diagnosis and the metabolic disturbances associated with it.
7.1. Digestion of proteins: in stomach (gastric HCl, pepsin and rennin), in small intestine [(pancreatic enzymes: trypsin, chymotrypsin, elastase and carboxypeptidase) and intestinal enzymes (aminopeptidase, tripeptidases and dipeptidases)].
7.2. Absorption of amino acids: the sodium-amino acids carrier system and g-glutamyl cycle.
7.3. Fate of absorbed amino acids
7.4. General aspect of amino acid metabolism: dietary proteins and amino acids, essential, semi-essential and non-essential amino acids, biological value of proteins, protein turnover, dietary protein requirement, calorigenic value of proteins, nitrogen balance.
7.5. Endocrine influence on protein metabolism: insulin, growth hormone, thyroid hormones, androgens and corticoids.
7.6 Removal of amino acid nitrogen: transamination [alanine transaminase (ALT), aspartate transaminase (AST) and glutamate transaminase]. Deamination; oxidative deamination, transdeamination and pecific deamination for specific amino acids.
7.7. Urea formation: site and steps, regulation of urea synthesis and hyperammonemia.
7.8. Metabolism of ammonia: sources, fate, removal and excretion of ammonia.
7.9. Metabolism of creatine: synthesis of creatine, blood creatine and creatinine, excretion of creatine and creatinine and creatinuria (physiological and pathological creatinuria).
7.10. Metabolic fate of amino acid carbon skeletons: pure glucogenic, pure ketogenic and mixed amino acids,
7.11. Metabolism of individual amino acids: synthesis of non-essential amino acids, the glucogenic or ketogenic pathways, functions and important derivatives and metabolic inborn errors of each amino acid (glycine, alanine, serine, threonine, cysteine, methionine, valine, leucine and isloleucine, aspartate, glutamate, arginine, lysine, phenylalanine and tyrosine, tryptophan, histidine, proline and hydroxyproline)
By the end of this course the student should be able to know how are proteins digested and absorbed, and the diseases which may result from defects in these processes. He should also appreciate the difference between various proteins which maintain the body in nitrogen equilibrium He should understand the overall metabolism of nitrogen as well as the states of posi- tive balance, negative balance and equilibrium of nitrogen.
The student should understand the different mechanisms by which amino acids are deaminated and the fate of the products of deamination. He should also comprehend the effect of hormones on protein metabolism
The student should learn how the nonessential amino acids are synthesized by humans and how are active amines and other important metabolites formed from amino acids.
He should understand how are individual amino acids metabolized through specific pathways so as to appreciate the different types of inborn errors of metabolism resulting from defects in the metabolism of these amino acids. The functions, synthesis and catabolism of creatine as well as causes of creatinuria should be well understood. In addition to the pathways which correlate carbohydrates, fats and proteins.
8.1. Synthesis of porphyrins and heme: synthesis of d-aminolevulinate (ALA), synthesis of porphobilinogen (PBG) and synthesis of different porphyrins and heme, porphyria (enzyme defects and main symptoms) and lead poisoning.
8.2. Catabolism of heme: formation of bilirubin in reticuloendothelial system, uptake and excretion by liver and changes in large intestine. Plasma bilirubin or bile pigments, normal levels (indirect reacting or unconjugated bilirubin and direct reacting or conjugated bilirubin).
8.3. Hyperbilirubinemia: unconjugated and conjugated hyperbilirubinemia, clinical classification into prehepatic (or hemolytic), hepatic and obstructive jaundice.
By the end of this course the student should be able to understand how heme is synthesized and to appreciate the importance of this to the causation of the porphyrias. He should also understand the catabolism of heme as well as the relation of this to the development of jaundice.
9. METABOLISM OF PURINE AND PYRIMIDINE NUCLEOTIDES
9.1. Digestion of nucleic acids
9.2. Purine metabolism:
9.2.1. Biosynthesis of purines; de novo synthesis (the sources of different atom of purine ring, synthesis of PRPP, synthesis of phosphoribosylamine, synthesis of inosine monophosphate (IMP), conversion of IMP to AMP and GMP). Synthesis of nucleoside di and triphosphates. Synthesis of deoxyribonucleotide. Purine salvage system (salvage of free purines and of purine nucleosides). Regulation of biosynthesis of purine nucleotides.
9.2.2. Catabolism of purines: uric acid formation, gout or hyperuricemia [metabolic gout (primary and secondary metabolic gout) and renal gout (primary and secondary renal gout) and treatment of gout. Hypouricemia; xanthine oxidase deficiency, adenosine deaminase (ADA) deficiency and purine nucleoside phosphorylase deficiency.
9.3. Pyrimidine metabolism
9.3.1. Biosynthesis of pyrimidines: the sources of different atoms of the pyrimidine ring, de novo synthesis, pyrimidine salvage system, regulation of pyrimidine nucleotide biosynthesis and orotic aciduria.
9.3.2. Catabolism of pyrimidines
9.4. Synthetic base analogs: antitumor drugs, antiviral drugs and allopurinol.
By the end of this course the student should be able to understand how are purines synthesized, the importance of this for cell maturation and multiplication, and how may inhibition of this may be used in the treatment of cancers. He should also be able to understand how may excessive production and catabolism of purines lead to gout and how may this disease be handled. The causes of hypouricemia and its relation to immune deficiency should also be apprehended.
By the end of this course the student should be able to understand how are pyrimidines synthesized, the importance of this for cell maturation and multiplication, and how may inhibition of this be used in the treatment of cancers. He should also be able to understand how disorders in pyrimidine metabolism lead to disease.
10. BIOCHEMICAL CHANGES IN LARGE INTESTINE
10.1 Intestinal fermentation
10.2. Intestinal putrefaction: reductive deamination and decarboxylation.
By the end of this course the student learns to appreciate the importance of intestinal bacteria. He should also understand how may defective digestion and absorption affect the composition of feces.
11. METABOLISM OF XENOBIOTICS (DETOXIFICATION)
11.1. Phase one: it includes oxidation (or hydroxylation ), reduction and hydrolysis.
11.2. Phase two: The product of phase one is conjugated to other polar compounds to increase their solubility in water and to facilitate their excretion.
11.3. Oxidation and hydroxylation: primary alcohols and aromatic compounds.
11.4. Reduction
11.5. Hydrolysis
11.6. Conjugation with: glucuronic acid, phosphoadenosine-5`-phosphosulfate (PAPS) and amino acids (cystiene, glycine and glutamine).
By the end of this course the student should understand the different mechanisms by which the body gets rid of various types of foreign organic substances, particularly drugs and some products of metabolism.
12.1. Classification of vitamins: fat soluble vitamins (vitamin A, D, E & K) and water soluble vitamins (vitamin C & B complex).
12.2. Fat soluble vitamins
12.2.1. Vitamin A (retinol or antixerophthalmia): chemistry, sources, pro vitamin A (carotenoids), absorption, storage and transport, functions and deficiency manifestations, biochemistry of vision (rhodopsin cycle ), requirements and carotenemia.
12.2.2. Vitamin D (calciferol or antirickets ): chemistry, sources, calcitriol synthesis, functions and deficiency manifestations, rickets and osteomalacia, renal rickets, vitamin D resistant rickets (congenital hypophosphatemia), requirements and hypervitaminosis D.
12.2.3. Vitamin E (tocopherols or rat antisterility vitamin): chemistry, sources, antioxidant functions, deficiency manifestations and requirements.
12.2.4. Vitamin K (anti-hemorrhage vitamin): chemistry (vitamin K1, K2 & K3), functions, causes of deficiency and deficiency manifestations, effect of dicumarol and warfarin (vitamin K cycle) and requirements.
12.3. Water soluble vitamins
12.3.1. Vitamin C (L- ascorbic acid or antiscurvy): chemistry, sources and metabolism, functions, deficiency manifestations, requirements and excessive vitamin C.
12.3.2. Vitamin B complex: animal and plant sources
12.3.3. Thiamine (vitamin B1 or anti- Beri Beri ): chemistry, functions of TPP, deficiency Manifestations
requirements,
12.3.4. Riboflavin (vitamin B2): chemistry, functions of riboflavin-phosphate (flavin mononucleotide or FMN) and flavin adenine dinucleotide (FAD), deficiency manifestations and requirements.
12.3.5. Nicotinic acid (niacin) (pellagra preventive factor or PPF), chemistry, synthesis from tryptophan, functions nicotinamide adenine dinucleotide (NAD+) and nicotinamide adenine dinucleotide phosphate (NADP+), deficiency manifestations and requirements
12.3.6. pyridoxine (Vitamin B6): chemistry, functions of PLP, deficiency manifestations and requirements.
12.3.7. Pantothenic acid: chemistry, functions, 4`-phosphopantotheine and CoA-SH, deficiency manifestations, requirements.
12.3.8. Biotin: chemistry, functions as CO2-carrier in CO2 fixation reactions (formation of CO2-biotin-enzyme complex), deficiency manifestations and requirements.
12.3.9. Folic acid: chemistry, activation of folic acid (folate), metabolism of one-carbon units, requirements and folate antagonists (anticancer drugs and antibacterial drugs).
12.3.10. Cobalamins (vitamin B12) (anti-pernicious anemia factor): chemistry, absorption, transport and storage of B12, functions, deficiency manifestations and requirements.
By the end of this course the student should appreciate the difference between the water-soluble and the fat-soluble vitamins. He should have an idea about the general properties and sources of each group of vitamins. He should apprehend their structure and function and should grasp well their deficiency manifestations as well as the hazards of excessive intake.
13.1. Principal elements ( macronutrients): they include 7 elements: calcium, phosphorus, magnesium, sodium, potassium, chlorine and sulfur.
13.2. Trace elements (micronutrients)
13.2.1. Essential trace elements: this group includes; iron, copper, zinc, manganese, iodine, cobalt, molybdenum, selenium, chromium and fluorine.
13.2.2. Possibly essential trace elements: this group includes; nickel, tin, vanadium and silicon.
13.2.3. Non-essential trace elements: this group includes; aluminum, boron, germanium, cadmium, arsenic, lead and mercury.
13.3. Calcium: dietary sources, absorption, factors affecting calcium absorption, distribution of calcium, blood calcium (plasma calcium), regulators of plasma calcium level (parathyroid hormone (PTH), calcitriol and calcitonin), disorders of plasma calcium (hypercalcemia and hypocalcemia), functions of calcium, role of calmodulin, excretion of calcium and requirements.
13.4. Phosphorus: dietary sources, absorption, distribution and functions, blood phosphate level (plasma inorganic phosphate), causes of hyperphosphatemia and hypophosphatemia, and requirements.
13.4. Magnesium: dietary sources, absorption, distribution and functions, blood magnesium level, causes of hypomagnesemia and hypermagnesemia, excretion and requirements.
13.5. Sodium: dietary sources, distribution and functions, blood or serum sodium Levels, causes of hypernatremia and hyponatremia, excretion and requirements.
13.6. Potassium: dietary sources, distribution and functions, blood or serum Potassium, causes Of hyperkalemia and hypokalemia, excretion and requirements
13.7. Chlorine: dietary sources, distribution and functions, abnormalities of chloride metabolism.
13.8. Sulfur: dietary sources, distribution and functions, organic sulfur compounds, inorganic sulfate compounds, excretion and requirements.
13.9. Iron: dietary sources, absorption, factors affecting iron absorption, transport in plasma (total iron binding capacity or TIBC), distribution, metabolism, abnormalities of iron metabolism, iron deficiency anemia, hemosiderosis (hemochromatosis) and requirements.
13.10. Copper: dietary sources, distribution and functions, blood copper, excretion, requirements and copper deficiency [menkes disease (kinky or steely hair disease) and Wilson disease (hepatolenticular degeneration)].
13.11. Iodine: dietary sources, absorption, distribution and functions, excretion, requirements and iodine deficiency.
13.12. Manganese: dietary sources, distribution and functions and requirements.
13.13. Zinc: dietary sources, absorption, distribution and functions, requirements and zinc deficiency.
13.14. Fluorine: distribution, functions and fluorosis.
13.15. Selenium: distribution and functions.
13.16. Cobalt: distribution and functions.
13.17. Molybdenum: distribution and functions.
13.18. Chromium: distribution and functions.
13.19. Aluminum: distribution and functions.
13.20. Boron: distribution and functions.
13.21. Cadmium: distribution and functions.
By the end of this course the student should be able to understand the sources, absorption, distribution, functions and excretion of these minerals. He should be able to comprehend how their deficiency or excess may cause disease.
14.1 Blood:
14.1.1. Blood cells: platelets and leukocytes in short.
14.1.2. Red blood cells: composition of RBC's (organic and inorganic constituents), metabolism of erythrocytes (glycolysis, energy production and HMP), carbonic anhydrase enzyme, rhodanese (cyanide sulfur transferase) and abnormalities of red cell (favism, pyruvate kinase deficiency, hereditary spherocytosis and abnormalities of hemoglobin).
14.1.3. Plasma: Plasma proteins, non-protein nitrogenous compounds, carbohydrates, lipids, ketone bodies, bile pigments, inorganic constituents and clinical Importance of plasma enzymes (transaminases, lactate dehydrogenase, amylase, alkaline phosphatase, acid phosphatase, choline esterase and creatine phosphokinase).
14.2. Urine: Urine formation in short, non-protein nitrogenous compounds, abnormal constituents of urine (proteins, sugars, ketone bodies, bile pigments and bile salts), urinary sediments [organised urinary sediments and unorganised urinary sediments (phosphates, calcium oxalate, urates) and urinary stones.
By the end of this course the student should be able to know the composition and metabolism of the red blood cells and the metabolic disturbances which may lead to hemolysis. He should also understand the composition of the plasma and appreciate the changes in different components (e.g. proteins, NPN compounds, etc.) in different diseases.
By the end of this course the student should understand the physical and chemical properties of urine. He should understand the normal and abnormal constituent of urine and their relation to different abnormalities of body metabolism and disease.