8 research outputs found
Effect of the Deletion of the (173â280) Fragment of the Inserted α-Helical Domain on the Functional Properties of ĐйР-Dependent Lon Protease from E. coli
No full textTHE PRINCIPAL DIFFERENCE IN REGULATION OF THE CATALYTIC ACTIVITY OF WATER-SOLUBLE AND MEMBRANE FORMS OF ENZYMES IN REVERSED MICELLES - GAMMA-GLUTAMYL-TRANSFERASE AND AMINOPEPTIDASE
No full textThe 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 an examples of gamma-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 >
THE PRINCIPAL DIFFERENCE IN REGULATION OF THE CATALYTIC ACTIVITY OF WATER-SOLUBLE AND MEMBRANE FORMS OF ENZYMES IN REVERSED MICELLES - GAMMA-GLUTAMYL-TRANSFERASE AND AMINOPEPTIDASE
No full textThe 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 an examples of gamma-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 >
Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domains
No full text
Unconventional serine proteases: Variations on the catalytic Ser/His/Asp triad configuration
No full text
