PHYSICOCHEMICAL PROPERTIES OF COLLAGENOLYTIC PROTEASE-C OF THE KAMCHATKA CRABстатья
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Дата последнего поиска статьи во внешних источниках: 29 мая 2015 г.
Местоположение издательства:Road Town, United Kingdom
Первая страница:28
Последняя страница:32
Аннотация:The collagenolytic protease C from the hepatopancreas of the Kamchatka crab was shown to be capable of effectively hydrolyzing both native collagen and Bz-Tyr-OEt at physiological pH values. The specific activity of this protease with respect to insoluble collagen and Bz-Tyr-OEt is equal to 300 and 5.4 units per mg protein, respectively. The molecular weight of protease C, measured by electrophoresis in gradient polyacrylantide gel (7-18%) in the presence of SDS and 2-mercaptoethanol, is equal to 24 kD. The amino acid composition of isoenzymes A and C of the collagenolytic crab proteases were determined. Isoenzyme C was found to exhibit maximum activity at alkaline pH values. The catalytic constants of the hydrolysis of Bz-Tyr-OEt and Bz-Arg-pNA in the presence of crab protease C were estimated. A study of the influence of various inhibitors on the protease C activity permitted the enzyme isolated to be classified as a serine protease.