Enzymology, the second 1400-215ENZ2
This practical course deals with the modern laboratory methods of enzyme research and their application in biotechnology. The several methods of enzyme purification, including centrifugation, ion-exchange, affinity chromatography and electrophoresis are used. Enzyme activities are followed with the use of spectrophotometric methods. Students should perform four laboratory experiments of the enclosed list:
1. Isolation and purification of either yeast glucose-6-phosphate dehydrogenase. Purification protocol;
2. Estimation of kinetic parameters for lactate dehydrogenase;
3. Photosynthetic complexes as an example of multienzyme system;
4. The action of activators and inhibitors on enzyme activity - Co-factor-induced changes in papaine.
5. Computer simulation of enzymatic kinetics
The protocols are compiled in electronic version, as a Word and Excel files.
Type of course
Mode
Prerequisites (description)
Course coordinators
Learning outcomes
Anticipated course effects
a) konwledge in the enzymology, especially in measurements and calculation of kinetics experiments
b) laboratory skilfulness eg. spectophotometry, electrophoresis, enzymes isilation
c) skilfulness in computer data analysis
Assessment criteria
A mark for course included
a) marks for raports from experiments, prepared by students as a computer files
b) oral presentation of selected data
c) written test from biochemical calculation
Mark for written final exam is independent on mark for course
Practical placement
N/A
Bibliography
A. Zgirski, R. Gondko Obliczenia Biochemiczne, PWN 1998
J.M Berg, J.L. Tymoczko, L. Stryer Biochemistry, Freeman and Co, 2002
Enzymatic base Brenda: http://www.brenda.uni-koeln.de/
Enzymatic base Expasy: http://www.expasy.ch/enzyme/
Base of IUBMB organization: http://www.chem.qmul.ac.uk/iubmb/
Additional information
Additional information (registration calendar, class conductors, localization and schedules of classes), might be available in the USOSweb system: