Course code: BIO-3300
Methods in biochemistry
Campus
Semester / Year
Autumn 2008
Credits
10
NOTE! This course belongs to a previous semester/year
BIO-3300
Methods in biochemistry
-10 ects
The course is administrated by
Faculty of Medicine
Faculty of Medicine
Type of course
This course can be taken as a singular course.
This course can be taken as a singular course.
Obligatory Prerequisites
BIO-1001 Cell and molecular biology
Course contents
This practical course revolves around four main topics that are explored using a spectrum of biochemical methods. After introductory lectures the laboratory work is carried out and the results are discussed in follow-up seminars. Topics for the exercises are: 1. Immunochemical analysis of immunoglobulins in egg yolk and of transferrin in blood using immunodiffusion, immunoelectrophoresis, miniature western blotting and EIA. 2. Highlighting structural and functional aspects of the blood clotting protein prothrombin, using affinity chromatography, electrophoresis and western blotting, and also comparative analysis of blood platelets and microparticles using 2D-electrophoresis. 3. Enzyme kinetical studies of alcohol dehydrogenase from yeast, using active site titration, velocity assay, inhibition and inactivation techniques, as well as group modifications. 4. Purification and binding studies of a transcription factor from zebra fish, expressed as a fusion protein in E.coli, using affinity purification (exploiting the fusion part), PCR, electrophoresis and gel retardation assay.
This practical course revolves around four main topics that are explored using a spectrum of biochemical methods. After introductory lectures the laboratory work is carried out and the results are discussed in follow-up seminars. Topics for the exercises are: 1. Immunochemical analysis of immunoglobulins in egg yolk and of transferrin in blood using immunodiffusion, immunoelectrophoresis, miniature western blotting and EIA. 2. Highlighting structural and functional aspects of the blood clotting protein prothrombin, using affinity chromatography, electrophoresis and western blotting, and also comparative analysis of blood platelets and microparticles using 2D-electrophoresis. 3. Enzyme kinetical studies of alcohol dehydrogenase from yeast, using active site titration, velocity assay, inhibition and inactivation techniques, as well as group modifications. 4. Purification and binding studies of a transcription factor from zebra fish, expressed as a fusion protein in E.coli, using affinity purification (exploiting the fusion part), PCR, electrophoresis and gel retardation assay.
Objective of the course
The course should give the student skills and insight into state of the art biochemical methods for biological and medical research.
The course should give the student skills and insight into state of the art biochemical methods for biological and medical research.
Language of instruction and examination
English
English
Teaching methods
16 hrs of lectures, 16 hrs of seminars, 88 hrs of lab work. The lab exercises are compulsory.
16 hrs of lectures, 16 hrs of seminars, 88 hrs of lab work. The lab exercises are compulsory.
Assessment methods
Evaluation of lab reports. Grade type: pass/ fail
Evaluation of lab reports. Grade type: pass/ fail
Course overlap
BIO-352 Biochemical methods 10
BIO-352AS Bioteknologiske arbeidsmetoder I 6
BIO-352 Biochemical methods 10
BIO-352AS Bioteknologiske arbeidsmetoder I 6
Recommended reading/syllabus
Compendium. Recommended reading: Principles and Techniques of Biochemistry and Molecular Biology by K Wilson and J Walker, (Cambridge University Press, Cambridge, 2005, 802 pp., ISBN 0-521-82889-9
Compendium. Recommended reading: Principles and Techniques of Biochemistry and Molecular Biology by K Wilson and J Walker, (Cambridge University Press, Cambridge, 2005, 802 pp., ISBN 0-521-82889-9
| Lectures Autumn 2008 Første oppmøte 25/8 kl 10.15, Aud 9, MH-bygget. |
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