ID:
510548
Duration (hours):
48
CFU:
6
SSD:
BIOCHIMICA
Year:
2025
Overview
Date/time interval
Secondo Semestre (02/03/2026 - 19/06/2026)
Syllabus
Course Objectives
The course aims to provide the student with the cognitive and methodological tools needed to:
- understand the theoretical principles underlying the main techniques for protein purification and analysis.
- understand the protocols for the production of polyclonal and monoclonal antibodies and for the production of recombinant proteins.
- understand the theoretical principles underlying the main techniques for DNA analysis and manipulation.
- understand the theoretical principles underlying the assays of the main biomarkers in clinical biochemistry.
At the end of the course, the student must:
- know the difference between the main protein and DNA analysis techniques;
- know the protocols for protein purification and the production of antibodies and recombinant proteins.
- know the theoretical principles underlying the assays of the main biomarkers used in clinical biochemistry.
- discuss independently the biochemical techniques to be used to solve experimental problems proposed during the examination.
Autonomy of judgement will be stimulated during the lectures.
- understand the theoretical principles underlying the main techniques for protein purification and analysis.
- understand the protocols for the production of polyclonal and monoclonal antibodies and for the production of recombinant proteins.
- understand the theoretical principles underlying the main techniques for DNA analysis and manipulation.
- understand the theoretical principles underlying the assays of the main biomarkers in clinical biochemistry.
At the end of the course, the student must:
- know the difference between the main protein and DNA analysis techniques;
- know the protocols for protein purification and the production of antibodies and recombinant proteins.
- know the theoretical principles underlying the assays of the main biomarkers used in clinical biochemistry.
- discuss independently the biochemical techniques to be used to solve experimental problems proposed during the examination.
Autonomy of judgement will be stimulated during the lectures.
Course Prerequisites
Understanding of the topics covered in the Applied Biochemistry with Fundamentals of Clinical Biochemistry course requires that the students posses the knowledge of Biochemistry concerning the structure and properties of amino acids and proteins. It is also required that the student be able to recognize the functional groups of the main organic compounds and the structure of heterocyclic compounds.
Teaching Methods
Frontal lectures.
Upon request, the lecturer is available for clarification of the topics covered in the lectures.
Lecture slides and further information are available on the KIRO platform.
For students with special needs, who are unable to attend teaching activities in person and who have applied for Inclusive Teaching Modalities, appropriate teaching materials will be available for fruitful self-study. If required, self-study may be supported by tutoring or supplementary teaching activities, and dedicated meetings, including online, with schedule flexibility as needed.
Upon request, the lecturer is available for clarification of the topics covered in the lectures.
Lecture slides and further information are available on the KIRO platform.
For students with special needs, who are unable to attend teaching activities in person and who have applied for Inclusive Teaching Modalities, appropriate teaching materials will be available for fruitful self-study. If required, self-study may be supported by tutoring or supplementary teaching activities, and dedicated meetings, including online, with schedule flexibility as needed.
Assessment Methods
Oral examination. The student will be stimulated to discuss experimental approaches described during the course to solve problems proposed by the lecturer.
An "in itinere" written examination is scheduled at the end of the course for students enrolled in the third year.
The test is considered passed with a score of no less than 18/30.
Appropriate examination formats are provided for students who fall into the categories provided for Specific Learning Disorders (SLD) and Special Educational Needs (SED).
An "in itinere" written examination is scheduled at the end of the course for students enrolled in the third year.
The test is considered passed with a score of no less than 18/30.
Appropriate examination formats are provided for students who fall into the categories provided for Specific Learning Disorders (SLD) and Special Educational Needs (SED).
Texts
Maccarone, Metodologie biochimiche e biomolecolari, Zanichelli, ISBN 978-88-08-52055-5
Bonaccorsi di Patti, Contestabile, Di Salvo, Metodologie biochimiche, Zanichelli, ISBN 978-88-08-52058-6
Nelson, Cox, Introduzione alla biochimica di Lehninger, Zanichelli, ISBN 9788808723284
Bonaccorsi di Patti, Contestabile, Di Salvo, Metodologie biochimiche, Zanichelli, ISBN 978-88-08-52058-6
Nelson, Cox, Introduzione alla biochimica di Lehninger, Zanichelli, ISBN 9788808723284
Contents
Techniques for tissue homogenization and separation of subcellular constituents. Protein extraction methods from different tissues and fractional precipitation: ammonium sulfate and isoelectric fractional precipitation; organic solvent precipitation; heat precipitation. Dialysis: principles and applications. Spectrophotometry: principles and applications. Lambert-Beer's law. Colorimetric assays.
Chromatographic techniques: general principles, chromatographic parameters and theoretical plates. Column chromatography. Adsorption and breakdown chromatography. Notes on TLC. Ion exchange chromatography. Gel filtration chromatography. Affinity chromatography. Hydrophobic interaction chromatography. High-performance liquid chromatography (HPLC): description of the various components of a high-performance chromatograph. Normal phase chromatography (NP-HPLC) and reversed phase chromatography (RP-HPLC). Ion coupling. Fast protein liquid chromatography (FPLC): principles and applications.
Electrophoretic techniques: general principles and factors affecting electrophoretic mobility. Free-phase electrophoresis: overview. Gel electrophoresis: SDS -PAGE and agarose gel electrophoresis. Western blotting. Hints at isoelectrofocusing and two-dimensional electrophoresis. Capillary electrophoresis.
Mass spectrometry: principles and applications. Electrospray ionization (ESI) and MALDI ionization. Quadrupole and time-of-flight (TOF) analyzer.
Monoclonal antibody production: hybridoma technique.
Hints on the structure, properties and function of nucleic acids. DNA and RNA synthesis. Function and reaction mechanisms of DNA and RNA polymerases. Control of gene expression in prokaryotes: lactose operon in E.coli.
Methods of DNA purification. Restriction enzymes: characteristics and applications in genome analysis. DNA electrophoresis. DNA amplification by PCR. Sanger's method for determining DNA sequence. Cloning techniques and expression of recombinant proteins.
Basics of biochemistry and clinical enzymology. Biochemical profiles of clinical relevance: glucose profile and assay methods; protein profile: plasma proteins and their functions, protidogram and disease states; lipid profile: main functions of plasma lipoproteins and cholesterol assay. Enzyme assay for diagnostic purposes: description of the main enzymes used in diagnostics, evaluation of their clinical significance and description of the assay method.
Chromatographic techniques: general principles, chromatographic parameters and theoretical plates. Column chromatography. Adsorption and breakdown chromatography. Notes on TLC. Ion exchange chromatography. Gel filtration chromatography. Affinity chromatography. Hydrophobic interaction chromatography. High-performance liquid chromatography (HPLC): description of the various components of a high-performance chromatograph. Normal phase chromatography (NP-HPLC) and reversed phase chromatography (RP-HPLC). Ion coupling. Fast protein liquid chromatography (FPLC): principles and applications.
Electrophoretic techniques: general principles and factors affecting electrophoretic mobility. Free-phase electrophoresis: overview. Gel electrophoresis: SDS -PAGE and agarose gel electrophoresis. Western blotting. Hints at isoelectrofocusing and two-dimensional electrophoresis. Capillary electrophoresis.
Mass spectrometry: principles and applications. Electrospray ionization (ESI) and MALDI ionization. Quadrupole and time-of-flight (TOF) analyzer.
Monoclonal antibody production: hybridoma technique.
Hints on the structure, properties and function of nucleic acids. DNA and RNA synthesis. Function and reaction mechanisms of DNA and RNA polymerases. Control of gene expression in prokaryotes: lactose operon in E.coli.
Methods of DNA purification. Restriction enzymes: characteristics and applications in genome analysis. DNA electrophoresis. DNA amplification by PCR. Sanger's method for determining DNA sequence. Cloning techniques and expression of recombinant proteins.
Basics of biochemistry and clinical enzymology. Biochemical profiles of clinical relevance: glucose profile and assay methods; protein profile: plasma proteins and their functions, protidogram and disease states; lipid profile: main functions of plasma lipoproteins and cholesterol assay. Enzyme assay for diagnostic purposes: description of the main enzymes used in diagnostics, evaluation of their clinical significance and description of the assay method.
Course Language
Italian
Degrees
Degrees
PHARMACY
Single-cycle Master’s Degree
5 years
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People
People
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