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Trypsin-like enzyme fromStreptomyces 771
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
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
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.
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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