The principal difference in regulation of the catalytic activity of water soluble and membrane forms of enzymes in reversed micelles. γ-Glutamyltransferase and aminopeptidase

S. N. Nametkin, A. V. Kabanov, G. N. Evtushenko, N. L. Klyachko, E. F. Kolesanova, T. V. Rotanova, N. N. Chernov, A. V. Levashov

Department of Chemical Enzymology, M. V. Lomonosov Moscow State University; Chair of Biochemistry, P. Lumumba State University, Moscow; M. M. Shemyakin Institute of Bioorganic Chemistry, Academy of Sciences of the USSR, Moscow

Abstract: The regulations of functioning of water soluble and membrane forms of enzymes in the systems of reversed micelles of surfactants in organic solvents are compared. By examples of γ-glutamyltransferase (in AOT reversed micelles in octane) and amino-peptidase (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 largely on the surfactant concentration at the constant hydration degree, 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 the enzyme's membrane activity”.

Russian Journal of Bioorganic Chemistry 1991, 17 (4):442-447

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