Unit GENERAL APPLIED AND CLINICAL BIOCHEMISTRY
- Course
- Industrial pharmacy
- Study-unit Code
- A003594
- Curriculum
- In all curricula
- Teacher
- Carmela Conte
- Teachers
-
- Carmela Conte
- Michela Codini (Codocenza)
- Hours
- 51 ore - Carmela Conte
- 36 ore (Codocenza) - Michela Codini
- CFU
- 10
- Course Regulation
- Coorte 2023
- Offered
- 2024/25
- Learning activities
- Caratterizzante
- Area
- Discipline biologiche e farmacologiche
- Academic discipline
- BIO/10
- Type of study-unit
- Obbligatorio (Required)
- Type of learning activities
- Attività formativa monodisciplinare
- Language of instruction
- Italian
- Contents
- Knowledge of the main biological macromolecules and the relationship between structure and function.
Metabolisms and related clinical aspects. Main biochemical methods for the study of macromolecules. - Reference texts
- - I principi di Biochimica di Lehninger Di
Nelson and Cox- Zanichelli Editore
- Biochimica Medica di Siliprandi e Tettamanti, Piccin editore. - Educational objectives
- At the end of the study the student will be able to acquire the basic knowledge of the fundamental principles of General, applied and clinical biochemistry.
- Prerequisites
- The course of general, applied and clinical biochemistry aims to address topics that the student will be able to learn if he has acquired the basic knowledge of inorganic and organic chemistry. In order to understand the contents of the course, it is essential that the student has acquired the fundamental notions on the structure of the main macromolecules and chemical bonds as well as their behavior during metabolic reactions.
- Teaching methods
- Teaching will be carried out through lectures in the classroom covering all the topics of the program and exercises for the applied biochemistry part which will take place in the laboratory.
- Other information
- none
- Learning verification modality
- The evaluation includes a single oral test during which the student will have to answer questions regarding the topics covered during the lessons and exercises. During the interview the student will have to demonstrate coherence with the proposed question, clarity of presentation and adequate scientific terminology
- Extended program
- Structure and function of the main biomolecules.
Nucleic acids: DNA and RNA
Carbohydrates: monosaccharides, disaccharides and polysaccharides and their implications in human biochemistry.
Evaluation of glucose metabolism. Diabetes. Glycated hemoglobin.
Lipids: the main classes of lipids and their implications in human biochemistry.
Dyslipidemias. Plasma lipoproteins. Classification of lipoproteins based on density and electrophoretic migration. The apolipoproteins. Chylomicrons: structure, function and fate. VLDL: structure, function and fate. Structure, function and fate of LDL. HDL: structure and function. atherosclerotic plaques..
Amino acids. Classification and description of the twenty alpha-L-amino acids that constitute the proteins. Essential amino acids. Other amino acids of metabolic importance.
Proteins. Functions performed by proteins in the human organism. The structure of proteins. The peptide bond. Amino acid sequence. Secondary structure and description of the alpha-helix, beta-sheet and beta-folds. Structural reasons. Tertiary structure. Forces that stabilize the three-dimensional structure of proteins. Structural domains. Quaternary structure. Globular proteins and fibrous proteins. Alpha-keratins and silk fibroin. Protein study methods.
Protein folding. Incorrect protein folding. Post-translational modifications of proteins: glycosylation and phosphorylation. Lipid anchors. Peptide signaling. Intracellular trafficking of proteins. Protein degradation. Ubiquitination system. The proteasome.
- Alteration of the metabolism of nitrogenous compounds: azotemia, uremia, uricemia
Connective tissue proteins. Collagen: triple helix, proline-hydroxyproline (role of vitamin C). Collagen Proteoglycans. Blood: hemochromocytometric test. Wintrobe indices, Hematocrit, Leukocyte count, ESR, Iron, anemia
The globines. Structure of myoglobin and hemoglobin; relationships between structure and function. Hemoglobinopathies.
General information on enzymes: Classification, catalytic activity and structure; cofactors and prosthetic groups; holoenzyme and apoenzyme. Specificity of action. Formation of the enzyme-substrate complex. Features of the active site. Enzyme kinetics. Michaelis and Menten model. Km and Vmax values. Unit of measurement of enzymatic activity. Reversible enzymatic reactions. Effect of pH and temperature. Competitive, non-competitive and irreversible inhibition. Drugs such as enzyme inhibitors. Mechanisms of enzymatic catalysis. Acid-base catalysis. Covalent catalysis. Multienzyme complexes: pyruvate dehydrogenase.
Enzyme regulation. Allosterism and cooperativeness. Kinetics of allosteric enzymes. Cooperation: concerted model and sequential model. Covalent regulation: reversible and irreversible. Signal amplification: blood clotting. Compartmentalization. Control of the intracellular level of enzymes.
Clinical enzymology. Liver function indices
Biochemical action of vitamins. Vitamins used in metabolic pathways. Water-soluble and fat-soluble vitamins. Vitamin needs and deficiencies. Coenzymes: structure and functions. Flavin and pyrimidine coenzymes. Folic acid. Thiamine. Lipoic acid. Biotin. Coenzyme A. Pyridoxine coenzymes. Vitamin B12 coenzymes.
Cell membranes and transmembrane transport. Membrane phospholipids. Membrane proteins. Asymmetry of the plasmalemma. The erythrocyte membrane. Spectrin and glycophorin. Transmembrane transport: classification. Selective permeability. Passive transport and active transport. The ATPases. Molecular model of the Na+/K+ ATPase.
- Practical exercises: Study of proteins. From extraction to quantification. - Obiettivi Agenda 2030 per lo sviluppo sostenibile
- health and wellness