Isolation and characteristics of trypsin from pyloric ceca of the starfish Asterina pectinifera.

نویسندگان

  • Hideki Kishimura
  • Kenji Hayashi
چکیده

Trypsin was purified from pyloric ceca of the starfish Asterina Pectinifera by ammonium sulfate precipitation, gel filtration, and cation-exchange chromatography. Final enzyme preparation was nearly homogeneous in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and its molecular weight was estimated as approximately 28000. Optimum pH and temperature of A. pectinifera trypsin for hydrolysis of N(alpha)-p-Tosyl-L-arginine methyl ester hydrochloride were approximately pH 8.0 and 55 degrees C, respectively. A. pectinifera trypsin was unstable at above 50 degrees C and below pH 5.0, and was not activated by adding Ca(2+). The N-terminal amino acid sequence of A. pectinifera trypsin, IVGGHEF, was found.

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منابع مشابه

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عنوان ژورنال:
  • Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology

دوره 132 2  شماره 

صفحات  -

تاریخ انتشار 2002