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 students with the theoretical and methodological knowledge required to understand the main biochemical techniques used for the analysis of proteins, nucleic acids and clinically relevant biomarkers. The course also introduces the conceptual basis of methodologies used for antibody production and recombinant protein expression.
Knowledge and understanding.
At the end of the course students are expected to acquire knowledge of the theoretical principles underlying the main techniques for protein purification and analysis, the protocols used for the production of polyclonal and monoclonal antibodies and recombinant proteins, as well as the main techniques for DNA analysis and manipulation. Students should also understand the theoretical principles underlying the measurement of the main biomarkers used in clinical biochemistry.
Applying knowledge and understanding.
Students should be able to distinguish between the main techniques used for protein and DNA analysis, understand the basic protocols for protein purification and for the production of antibodies and recombinant proteins, and interpret the methodological principles underlying the main biochemical tests used in clinical practice.
Making judgements.
Students should be able to critically discuss and independently evaluate the most appropriate biochemical techniques to address experimental problems proposed during the examination. The development of independent judgement will be encouraged during lectures through discussion of the principles and applications of biochemical methodologies.
Communication skills.
Students should be able to use appropriate scientific terminology related to applied biochemistry and clinical biochemistry to describe techniques, experimental protocols and methodological principles.
Learning skills.
Students should acquire the basic knowledge necessary to further explore biochemical methodologies used in biomedical research and laboratory diagnostics.
Knowledge and understanding.
At the end of the course students are expected to acquire knowledge of the theoretical principles underlying the main techniques for protein purification and analysis, the protocols used for the production of polyclonal and monoclonal antibodies and recombinant proteins, as well as the main techniques for DNA analysis and manipulation. Students should also understand the theoretical principles underlying the measurement of the main biomarkers used in clinical biochemistry.
Applying knowledge and understanding.
Students should be able to distinguish between the main techniques used for protein and DNA analysis, understand the basic protocols for protein purification and for the production of antibodies and recombinant proteins, and interpret the methodological principles underlying the main biochemical tests used in clinical practice.
Making judgements.
Students should be able to critically discuss and independently evaluate the most appropriate biochemical techniques to address experimental problems proposed during the examination. The development of independent judgement will be encouraged during lectures through discussion of the principles and applications of biochemical methodologies.
Communication skills.
Students should be able to use appropriate scientific terminology related to applied biochemistry and clinical biochemistry to describe techniques, experimental protocols and methodological principles.
Learning skills.
Students should acquire the basic knowledge necessary to further explore biochemical methodologies used in biomedical research and laboratory diagnostics.
Course Prerequisites
Understanding the topics covered in the Applied Biochemistry course requires basic knowledge of biochemistry, particularly the structure and properties of amino acids and proteins, as well as basic concepts of organic chemistry, including the main functional groups and the structure of heterocyclic compounds.
Teaching Methods
The course includes face-to-face lectures.
Lecture slides and other information will be available on the KIRO platform throughout the course.
Upon request, the lecturer is available for clarification of the topics covered in the lectures.
For students with specific needs who cannot attend classes in person and have applied for Inclusive Teaching Methods, suitable teaching materials will be made available for effective independent study. If requested, self-study can be supported by dedicated meetings with flexible scheduling based on individual needs.
Lecture slides and other information will be available on the KIRO platform throughout the course.
Upon request, the lecturer is available for clarification of the topics covered in the lectures.
For students with specific needs who cannot attend classes in person and have applied for Inclusive Teaching Methods, suitable teaching materials will be made available for effective independent study. If requested, self-study can be supported by dedicated meetings with flexible scheduling based on individual needs.
Assessment Methods
Student assessment consists of a final oral examination. During the exam, students will be asked to discuss and evaluate experimental approaches that could be used to address problems proposed by the instructor, demonstrating their ability to apply the theoretical knowledge acquired to the main methodologies of applied and clinical biochemistry.
At the end of the course, an intermediate assessment is also scheduled for students enrolled in the third year. The examination is considered passed with a minimum grade of 18/30.
Appropriate examination arrangements are provided for students with Specific Learning Disorders (SLD) and Special Educational Needs (SEN), in accordance with current regulations and university guidelines.
At the end of the course, an intermediate assessment is also scheduled for students enrolled in the third year. The examination is considered passed with a minimum grade of 18/30.
Appropriate examination arrangements are provided for students with Specific Learning Disorders (SLD) and Special Educational Needs (SEN), in accordance with current regulations and university guidelines.
Texts
Maccarone, Metodologie biochimiche e biomolecolari, Zanichelli.
Bonaccorsi di Patti, Contestabile, Di Salvo, Metodologie biochimiche, Zanichelli,
Albi E. Biochimica Clinica Essenziale. Zanichelli
Bonaccorsi di Patti, Contestabile, Di Salvo, Metodologie biochimiche, Zanichelli,
Albi E. Biochimica Clinica Essenziale. Zanichelli
Contents
The course programme is divided into three sections:
1) Methodologies for protein purification and analysis:
-Extraction of proteins from the biological source: cell disruption and tissue homogenisation.
-Fractionation methods for protein mixtures.
-Chromatographic methods. General principles. Gel-filtration, ion exchange, affinity chromatography. High pressure liquid chromatography (HPLC).
-Spectroscopic methods for studying proteins: UV-VIS absorption spectroscopy and Lambert and Beer's Law
-Electrophoretic techniques for studying proteins: SDS-PAGE polycrylamide gel electrophoresis, Western blot, capillary electrophoresis
-Mass spectrometry techniques: MALDI and ESI
-Polyclonal and monoclonal antibody production techniques
2) Hints on the structure, properties and function of nucleic acids:
-DNA and RNA synthesis
-Function and reaction mechanism of DNA and RNA polymerases
-Regulation of DNA transcription: lactose operon in E. coli
3) Methodologies for DNA and RNA extraction and purification.
-Cell lysis by mechanical, chemical or enzymatic methods
-Spectrophotometric methods for quantification of extracted nucleic acids
-Electrophoretic methods for analysing nucleic acids
-Amplification of a portion of DNA by PCR technique
-DNA sequencing method
-Recombinant DNA technique for the production of recombinant proteins
4) 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.
1) Methodologies for protein purification and analysis:
-Extraction of proteins from the biological source: cell disruption and tissue homogenisation.
-Fractionation methods for protein mixtures.
-Chromatographic methods. General principles. Gel-filtration, ion exchange, affinity chromatography. High pressure liquid chromatography (HPLC).
-Spectroscopic methods for studying proteins: UV-VIS absorption spectroscopy and Lambert and Beer's Law
-Electrophoretic techniques for studying proteins: SDS-PAGE polycrylamide gel electrophoresis, Western blot, capillary electrophoresis
-Mass spectrometry techniques: MALDI and ESI
-Polyclonal and monoclonal antibody production techniques
2) Hints on the structure, properties and function of nucleic acids:
-DNA and RNA synthesis
-Function and reaction mechanism of DNA and RNA polymerases
-Regulation of DNA transcription: lactose operon in E. coli
3) Methodologies for DNA and RNA extraction and purification.
-Cell lysis by mechanical, chemical or enzymatic methods
-Spectrophotometric methods for quantification of extracted nucleic acids
-Electrophoretic methods for analysing nucleic acids
-Amplification of a portion of DNA by PCR technique
-DNA sequencing method
-Recombinant DNA technique for the production of recombinant proteins
4) 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 (2)
Teaching staff
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