The principal difference in regulation of the catalytic activity of water‐soluble and membrane forms of enzymes in reversed micelles

FEBS Letters

Kabanov, Alexander V.¹  Levashov, Andrey V.¹  Nametkin, Sergey N.¹ 

[1] Department of Chemical Enzymology, Moscow State University, Moscow, USSR

关键词: Aminopeptidase;    γ-Glutamyltransferase;    Micellar enzymology;    Reversed micelle;    AOT;    aerosol OT (sodium bis(2-ethylhexyl)sulfosuc-cinate);    Brij 96;    oleyl poly(10)oxyethylene ether;    Triton X-100;    (4-octyl)phenol poly(9-10)ethylene glycol;    NA;    (4-nitro)aniline;    CNA;    (3-carboxy-4-nitro)aniline;    LeuNA;    L-Ieucyl(4-nitro)anilide;    GluNA;    γ-glutamyl(4-nitro)anilide;    GluCNA;    γ-glutamyl(3-carboxy-4-nitro)anilide;   

DOI  :  10.1016/0014-5793(90)80933-A

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown