Trypsin-like enzyme fromStreptomyces 771 |
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Authors: | V I Palubinskas N B Yankevich K K Yanulaitene V S Vesa V G Bendikene A V Maksimenko V P Torchilin E V Ilyina V N Smirnov I N Krestyanova Yu E Bartoshevich R Ch Zabirova |
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Institution: | (1) USSR Research Institute of Applied Enzymology, Vilnius, USSR;(2) USSR Research Center of Cardiology, Academy of Medical Sciences, Moscow, USSR;(3) USSR Research Institute of Antibiotics, Moscow, USSR |
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Abstract: | Electrophoretically homogenous proteolytic enzyme with molecular weight 31,500 and pI 3.75 was obtained from a culture medium
ofStreptomyces 771 by chromatography onN-benzyl chitin adsorbent, subsequent chromatography on CM-cellulose, and preparative isofocusing and chromatography on Sephadex
G-75. The enzyme hydrolyzesN- benzoyl-DL-arginine-p-nitroanilideN-benzoyl-DL-lysine-p-nitro-anilideN-benzoyl-DL-arginine ethyl ester, and Na-caseinate. It also exhibits pronounced thrombolytic activity. The activity of the enzyme was
suppressed by soya bean inhibitor, but remained unaffected by chelating agents and phenylmethylsulfonyl fluoride. The enzyme
was immobilized on aldehyde dextran, and some kinetic parameters of the immobilized enzyme were determined. The thrombolytic
activity of native and immobilized enzyme was studied as well. |
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Keywords: | Proteolytic enzyme from Streptomyces 771 chromatography of a proteolytic enzyme thrombolytic activity of a proteolytic enzyme soya-bean inhibitor of proteolytic enzyme immobilization of a trypsin-like enzyme aldehyde dextran immobilization of a proteolytic enzyme on dextran immobilization of a proteolytic enzyme on streptomyces 771 a trypsin-like enzyme from trypsin-like proteolytic enzyme from streptomyces 771 |
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