title: Isolation and characteristics of trypsin from pyloric ceca of the starfish Asterina pectinifera.
abstract: 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.
authors.affiliation: Graduate School of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido 041-8611, Japan. kishi@fish.hokudai.ac.jp
authors.forename: Hideki
authors.initials: H
authors.lastname: Kishimura
authors.forename: Kenji
authors.initials: K
authors.lastname: Hayashi
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002122:Calcium Chloride / Q000494:pharmacology; D002432:Cecum / Q000187:drug effects / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D011708:Pylorus / Q000187:drug effects / Q000201:enzymology*; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein; D017386:Sequence Homology, Amino Acid; D013215:Starfish / Q000187:drug effects / Q000201:enzymology*; D013696:Temperature; D014357:Trypsin / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*
chemical_list: D014357:Trypsin; D002122:Calcium Chloride