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The principal difference in regulation of the catalytic activity of water‐soluble and membrane forms of enzymes in reversed micelles
Author(s) -
Kabanov Alexander V.,
Nametkin Sergey N.,
Levashov Andrey V.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80933-a
Subject(s) - micelle , chemistry , pulmonary surfactant , catalysis , membrane , enzyme , cyclohexane , organic chemistry , chromatography , biochemistry , aqueous solution
The regularities of their functioning of enzyme, water‐soluble and membrane forms, in the systems of the reversed micelles of surfactants in organic solvents are compared. Using as examples γ‐glutamyltransferase (in AOT reversed micelles in octane) and aminopeptidase (in Brij 96 reversed micelles in cyclohexane), the principal difference in the catalytic activity regulation of water‐soluble and membrane forms is demonstrated. The catalytic activity of the membrane form depends considerably on the surfactant concentration at the constant degree of hydration, whereas the activity of the water‐soluble form is constant under these conditions. The catalytic activity dependence on the surfactant concentration is regarded as a test for enzyme membrane activity.