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1st Year Medical Chemistry Curriculum

(CHMMed-11) 1st  semester

Theory: 3 hours/week (3 Credits)

The primary goal of this course in general medical chemistry is to present the fundamental principles and chemical foundation essential to understanding physiological chemistry for students of medicine.
Throughout the course, chemistry is presented as an experimental science with biomedical examples in which theories evolve and change as new information is acquired to show how this vast science is applied to areas of interest to the medical students.

Theory Lectures

  • Radioactivity, radiation dosages medical uses of radioactive isotopes.
  • Gases & their medical relations and diffusion of respiratory gases.
  • Aqueous solutions, solubility, concentrations of solutions. Electrolytes & nonelectrolytes
  • Osmosis & osmotic pressure
  • Colloids and their properties, emulsions, emulsifying agents, dialysis, haemodialysis.
  • Acid and Bases, pH buffer acid-base balance in blood.
  • Reaction rate, activation energy chemical equilibrium.
  • Organic Chemistry: hyberdization, double & triple bonds, resonance. Alkanes.
  • Alkenes: geometric isomers, importance in living systems.
  • Aromatic compounds.
  • Stereoisomers: Chiral compounds, optical activity diastereomers, mesostereoisomers.
  • Alcohols: phenols, ethers, thiols.
  • Aldehydes & Ketones
  • Carboxylic acids: Esters & thioesters.

1st Year Practical Medical Chemistry

(CHMMed-p1) 1st  Semester

Three hours/ week (1.5 credit)


  • To introduce the students to the lab. Tools and equipments and train them how to handle these equipments.
  • To teach the student the safety procedures when dealing with chemicals and tools.
  • To enable the student to prove practically some of the theoretical scientific facts.
  • To make the student familiar with biochemical reaction (in-vivo & in-vitro).
  • To help the student to understand the basis of chemical and physiological processes.


Practical Lectures

  • General  laboratory apparatuses, safety procedures & first Aid
  • Analysis of silver group
  • Acid-Base titration:
  • The standardization of basic solutions.
  • Equivalent mass of an unknown acid.
  • pH & pH Meters
    • Osmosis & dialysis
    • Preparation of some colloids.
  • Determination of an unknown chloride.
  • The hydrolysis of methyl acetate with HCl catalyst.
  • The adsorption of acetic acid from aqueous solution by charcoal.
  • Aspirin synthesis & purification by re-crystallization.
  • A test for functional groups.
  • General urine examination.

1st Year Biochemistry Curriculum

(CHMBio-12) Second Semester

Theory: 2 hours/week (2 credits)


  • Biochemistry I, an introduction to the structure and function of biological molecules, is designed to study the molecules and macromolecules in living systems through an application of the principles of organic and physical chemistry. This will include an examination of the structure of and function of proteins, carbohydrates, lipids, hormones, trace elements in detail in order to understand how their unique chemical and physical properties contribute to their biological function.
  • The structures, specificities and kinetics of selected enzymes will illustrate the enormous diversity of this group of catalytic molecules.

Theory Lectures

  • Carbohydrate chemistry (4 hours)
    • Definition, classification, biological roles.
    • Monosaccharides, disaccharides, polysaccharides.
    • Mucopolysaccharides & glycoproteins.
  • Lipids (2 hours)
    • Definition & classification.
    • Fatty acids, prostaglandins.
    • Glycolipids, sphingolipids & lipoproteins.


  • Amino acid chemistry (2 hours)
  • Definition, classification, properties, & reactions.
  • Protein (4 hours)
  • Structure, conformation & denaturation.
  • Peptide bond, glutathione, insulin & glucagons.
  • Functional role: Hb, glycoprotein, collagen.
  • Protein technology.


  • Enzymes (4 hours)
  • Nature, nomenclature, & classifications & types of kinetic reactions.  
  • Mechanism of action, factors affecting enzyme activity, & control of activity.
  • Enzymes in diagnosis & therapy Definition, classification, chemistry & functions
  • Hormones (3 hours)
  • Definition, classification, chemistry & functions


  • Nutrition: and trace elements (3 hours)
  • Caloric values of food, basal metabolism, & nitrogen balance.
  • Protein energy malnutrition
  • Vitamins (2 hours)
  • Definition, classification.
  • Individual vitamin, chemistry, RDA & deficiencies


1st Year Practical Biochemistry

(CHMMed-P2) Second Semester

3 hours/week (1.5 credits)

This syllabus is designed to place greater emphasis on the understanding of the fundamentals of chemistry and application of scientific concepts and principles to develop abilities and skills that are relevant to the study and practice of medicine.

Practical Lectures

  • Carbohydrates: (Molish, Benedict, Barfoed, Bial, Seliwannof’s & Iodine Tests.)
  • Lipids: (Grease Stain Test, Reaction Test, Copper Acetate Test, Reaction of Soap, & Cholesterol)
  • Saponification Value of Fat.
  • Amino Acids & Proteins: (Ninhydrin, Xanthoprotic, Rosenheim, Millon’s, Lead Sulfide, Nitroprusside, Sakaguchi & Biurett Tests.)
  • Paper Chromatography of Amino Acids.
  • Spectrophotometry (Riboflavin).
  • Spectrophotometry (Albumin-Biurett).
  • Enzymes: The Determination of the Progress Curve of Casein by Trypsin.




2nd Year Biochemistry

(CHMBio-21) First Semester

Theory (3hours/week) (3 credits)


The biochemistry course is intended to give students of medicine a sound knowledge of metabolism which will guide them in acquiring sufficient information to increase their comprehension of how biochemically determinable constituents vary in normal and abnormal states, and to relate metabolic disorders to biochemical lesions.
It is intended to enlighten the students with recent advances in biochemical medicine and enable them to use available information to alleviate human suffering.

Theory Lectures

  • General aspects of metabolism (4 hours)
  • Energy cycles in nature, anabolism, catabolism, & regulation of metabolism.
  • Carbohydrate metabolism (12 hours)
  • Digestion, absorption of poly-, di-, & monosaccharides & disorders and membrane transport. Glycolysis, Coori cycle, & Krebs cycle.
  • Electron transport system (respiratory chain), oxidative phosphorylation & ATP synthesis.
  • Pentose phosphate shunt, pentose & NADPH synthesis, gluconeogenesis, glycogenesis, & glycogenolysis, & their regulation.


  • Lipid metabolism (8 hours)
  • Digestion & absorption of triglycerides, cholesterol & phospholipids, lipoprotein lipases, & synthesis of chylomicrones.
  • Beta oxidation of fatty acids, & energy production, propionate metabolism.
  • Synthesis of fatty acids, triglycerides, phospholipids, cholesterol, & fat storage.
  • Amino acids & protein metabolism (12 hours)
  • Protein: digestion, absorption, transport.
  • Amino acids:
  • Amino acid (glucogenic, ketogenic amino acids) degradation: catabolism of carbon skeleton 
  • Urea cycle & ammonia metabolism.
  • Amino acids biosynthesis & metabolic defects.
  • Hormones (9 hours)
  • Actions & regulatory control of hormones secretion.
  • Protein & amino acid derived hormones.
  • Anterior & posterior hormones.
  • Steriod hormones, structure & synthesis.
  • Sex hormones, secretion, action, regulation & disorders.

2nd Year Practical Biochemistry
(CHMBio-p1) First Semester

3 hours/week (1.5 Credits)


Practical biochemistry: Is a discipline that applies knowledge of basic biochemistry and analytical chemistry to the medical diagnosis, treatment and to the management of patients. It provides an objective base to assess the biochemical consequences of a particular pathological process and the response to the therapy.
It emphasis on the:

  • Origin and control of the biological and physiological variability of the biochemical data.
  • Biochemical bases and the clinical meaning of the great part of the tests done in a routine way with serum, plasma and other body fluids interpretive abilities, so that a graduate of medicine can use correctly the clinical analysis.

Practical Lectures

  • Introduction: lab. Hazards & sample collection.
  • Hemolysis of blood & pipetting techniques
  • Saliva: analysis of organic & inorganic constituents.
  • Determination of serum & salivary amylase activity.
  • Determination of serum glucose level.
  • Glucose tolerance test (GTT).
  • Determination of serum lipase activity.
  • Determination of serum cholesterol level.
  • Determination of S. total lipids & S. triglycerides values.
  • Determination of S. albumin, globulins, & A/G ratio.
  • S. proteins electrophoresis.
  • Determination of total hemoglobin.
  • Hemoglobin electrophoresis.
  • D-Xylose test.
  • Analysis of calculi.

2nd Year Clinical chemistry

(CHMBio-22) Second Semester

2 theory hours/week (2 Credits)



The program involves: changes during different disease states and general consequences. There is a stress on the:

  • Abnormal metabolism of macromolecules and pathological changes in the function of liver, kidney, different hormones with the clinical interpretation of laboratory findings.
  • Use of enzymes in clinical diagnosis and prognosis, isoenzymes, their clinical significance.
  • Porphyrin metabolism, and disorders, haemoglobinopathies, disorders of iron metabolism and significance of related laboratory tests.
  • Cancer chemistry and tumor markers and their importance in   clinical diagnosis and prognosis.


To have some experience in biochemical techniques in order to appreciate the practical problem of clinical biochemistry as a diagnostic tool and to improve the problem- solving skills through collaborative and individual reflection and analysis.

2nd Year Practical Clinical chemistry

(CHMBio-P2) Second Semester

3 hours/week (1.5 Credits)


This course involves practical study of renal function, liver function, electrolytes homeostasis, serum enzymes and their clinical significance, hemoglobin types (hemoglobinopathies). So, at the end of the course, student will be able to handle numerical data as a problem solving and diagnostic tool particularly for primary health care.


  • Determination of S. Urea
  • Determination of S. Creatinine & Creatinine Clearance
  • S. Electrolytes (S. K+  &  S. Na++)
  • Determination of S. Uric Acid.
  • Determination of S. Bilirubin.
  • Determination of S. Alkaline Phosphatase Activity
  • Determination of S. ALT & S. AST Activity
  • Determination of S. Inorganic Phosphate Level
  • Determination of S. Ca++ By Titration Method
  • Estimation of S. RNA Level
  • Determination of Acid Phosphatase Activity
  • Determination of S. Iron & Total Iron Binding Capacity
  • Atomic Absorption Spectrophotometry
  • Spectroflourometry  for S. Salicylate Level
  • Determination of S. LDH Activity




2nd Year Molecular Biology

(CHMMol-22) Second Semester

2 hours/week (2 Credits)

Molecular biology is a one- semester course designed to introduce students to the role of biological molecules in determining cellular function. Topics covered include a description of the structure and function of nucleic acids; the genetic code; protein biosynthesis and targeting; DNA replication and repair; recombinant DNA technology and genetic engineering; gene expression and its control; and signal transduction. Special topics include cell cycle regulation, apoptosis, and cancer. The format in the class is a combination of traditional lecture and problem- based learning.


The students will:

  • Acquire a familiarity with the nomenclature and vocabulary of molecular biology.
  • Understand the molecular basis of inherited diseases.
  • Be able to apply the principles of molecular biology in disease diagnosis (AIDS, TB,…….).
  • Appreciate the role of gene therapy in the treatment of inherited diseases.
  • Understand how PCR has led to the development of forensic medicine.
  • Be able to keep up with the information explosion in this field and appreciate the ongoing nature of research and the need for flexibility and modification of scientific knowledge.


1. DNA and RNA (2 hours)

  • Basic structure, components of nucleic acid, polarity, backbone,…..etc
  • General features of DNA double helix, viral nucleic acids & their Replication.

2. Flow of genetic information (2 hours)

  • Different kinds of cellular RNAs
  • Hybridization concept
  • General features of genetic code
  • Eucaryotic genes are interrupted genes
  • Exon shuffling and alternative splicing of RNA and their importance

3. Exploring genes (+ Recombinant DNA technology) (5 hours)

  • Definition of recombinant DNA technology
  • Practical application and importance of   recombinant DNA technology Restriction enzymes: types, characteristics, nomenclature, action,
  • Blotting techniques (southern, western, northern)
  • DNA sequencing methods
  • DNA probes: definition, synthesis and uses, DNA vectors
  • General concepts of PCR and its biomedical     application
  • Restriction fragment polymorphism
  • Chromosome walking,
  • Gene therapy and gene knockout
  • Prenatal diagnosis of some inherited diseases

4. DNA replication and repair (3 hours)

  • DNA grooves and B, A, and Z-helical forms
  • DNA topology: relaxed and superhelical forms, DNA gyrase and topoisomerases DNA polymerases and their action
  • Mechanism of DNA replication: synthesis of lagging and leading strands
  • Mutation and mutagenesis: definition, types, causes, mechanism, Ames test
  • Repair of DNA damage:
  • Etiological factors
  • Mechanism of repair
  • Xeroderma pigmentosa, molecular cause

5. Gene rearrangement (2 hours)

  • Recombination, integration: definition, mechanism, types, RecA and other elements in  mediating the processes
  • Transposition, and medically important transposons (R-plasmid, Insertion seq., Tn3..)
  • Immune diversity, class switching, and site specific recombination

6. RNA synthesis and splicing (2 hours)

  • RNA polymerases and their biological roles
  • Mechanism of transcription.
  • Post-transcriptional modification
  • Enhancer and promotors.
  • Antibiotic action on transcription process

7. Protein synthesis (3 hours)

  • Definition, initiators of protein synthesis
  • Wobble phenomena and t-RNA
  • Ribosomes and the mechanism of protein synthesis
  • Differences between procaryotic and eucaryotic translation process.
  • Antibiotic action on translation
  • Posttranslational modifications of protein

8. Protein targeting (2 hours)

  • Molecular signals and mechanisms for targeting of proteins to intracellular organelles (nucleus, mitochondrial compartments, peoxisomes, ER, …..)
  • Receptor-mediated endocytosis and its biological significance
  • Targeting proteins for destruction by ubiquitin

9. Control of gene expression in prokaryotes (2 hours)

  • Operon models for regulation of gene
  • Expression (lac operon, tryptophan operon,…..)
  • Control of translation of ribosomal proteins
  • Control of transcription in viruses

10. Eucaryotic chromosomes and gene expression (3 hours)

  • Structure of chromatin fibers
  • Eucaryotic DNA polymerases
  • Finishing of telomeres
  • Control on eukaryotic cell cycle
  • Mitochondrial DNA: distinctive feature and genetic codes
  • Repetitive DNA sequences and their importance
  • Hemoglobin gene structure in different developmental stages
  • Hormone -receptor gene interaction

11. Nucleotides (4 hours)

  • biomedical importance
    • unusual bases & their significance
    • synthetic nucleotide analogues & their medical importance
    • Metabolism of the purine & pyrimidine nucleotides
  • Denovo & salvage biosynthetic Pathways & their regulation
  • Catabolic pathways
  • Disorders of the purine & pyrimidine metabolism: hyperuricemia, orotic aciduia, adenosine deaminase deficiency,…..)