BIOCHEMISTRY II

Course Code:

4031-4032

Semester:

4th Semester

Specialization Category:

SBC

Course Hours:

5

ECTS:

5


Course Tutors

Trapali Maria

LEARNING OUTCOMES

At the end of this course the student will be able to:
● To know in depth the function of enzymes, what reactions they catalyze and by what mechanism.
● To know the kinetics of enzymes, the relevant equations and to be able to utilize with experimental data.
● To know the citric acid cycle, its products and the amount energy produced.
● To know glycolysis, Kalvin circle, glycogen metabolism
●To know fatty acid metabolism
● To know the biosynthesis of cholesterol and its chemical derivatives
● To know Hormone action.
● To know quality methods of identification of carbohydrates, fats and proteins / amino acids.
● To know methods of distinguishing amino acids by chromatography methods.
● To understand theoretically and experimentally the physical properties of proteins.

 

SYLLABUS

Theoretical lessons
● The structure of the enzymes. Classification and nomenclature of enzymes, reactions that are catalyzed. The Michaelis-Menten equation. The way of calculating V max, Km with experimental data and transformation of the equation.
● Allosteric and synergistic phenomena and related transformations of the Michaelis-Menten equation (Hill model, Adair etc.). The regulation of the action of the hymns, the proteolysis of homogeneous, protein kinase, phosphates, etc.
● The metabolism of proteins / amino acids, Decarboxylation, transaminosis, the oxidative deamination.
● The biosynthesis of essentials amino acids. The deamination and the formation of urea.
● Oxidative decarboxylation and the uric acid cycle.
● The metabolic role of porphyrins and their metabolism.
● Carbohydrate metabolism, glycolysis, gluconeogenesis. The starch and its metabolism. Photosynthesis.
●Lipids metabolism
●The production of steroid hormones, of carotenoids and vitamin D.
●The respiratory chain. Energy storage in membranes. The redox systems of the respiratory chain, the oxidative phosphorylation, the role of cytochromes.
● Hormones: Categories, place of production and mechanism of action, disorders.

 

Laboratory lessons
The laboratory part of the course includes practice in the following objects:
● Use of devices and instruments – Safety rules in the laboratory.
● Procedure and analytical calculations for laboratory exercise to determine pH of a buffer (initially and after addition of a strong acid or strong base)
● Qualitative determinations of sugars
● Qualitative determinations of amino acids. Titration, calculation of isoelectric point. Determination of pK1, pK2 and the pI of glycine.
● Qualitative assays of proteins. Physicochemical properties of proteins. Precipitation of proteins. Study of the effect of pH, temperature and ionic strength in their solubility.
●Protein Quantification-Bradford Method
● Spectrophotometry. The determination of λmax. The determination of Km, V max of a enzymatic reaction.
●Thin layer chromatography (TLC) of amino acids using ninhydrin.
●Thin layer chromatography (TLC) of amino acids using UV.