Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9602680 | Enzyme and Microbial Technology | 2005 | 13 Pages |
Abstract
Within the framework of classical Michaelis-Menten kinetics and in accordance with the customary use of KM for a comparison of enzyme-substrate affinity, the MCR parameter may be interpreted as a relative substrate affinity. This proportion remains nearly the same for different mould (or yeast) β-galactosidases, though the affinity to a particular substrate may vary essentially from enzyme to enzyme. The constancy of MCR may be a manifestation of structural similarity of binding sites for these enzymes.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Nataliya M. Samoshina, Vyacheslav V. Samoshin,