Abstract
A kind of trypsin-like enzyme was purified from crude extracts of pyloric caeca acetone powder of the starfish Asterias amurensis by the following methods; ammonium sulfate precipitation, gel filtration on Sephacryl S-200, and DEAE-cellulose column chromatography.The SDS-polyacrylamide gel electrophoresis pattern showed that the trypsin-like enzyme was homogeneous. Its molecular weight was estimated to be about 28, 000. The optimum pH and temperature of the trypsin-like enzyme for Tos-Arg-OMe hydrolysis were at around pH 8.0 and 5°C. The trypsin-like enzyme was unstable over 40°C or below pH 5.0, and was neither activated nor stabilized by calcium ions.
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