title: Anionic trypsin from chum salmon: activity with p-amidinophenyl ester and comparison with bovine and Streptomyces griseus trypsins.
abstract: An anionic trypsin from pyloric caeca of chum salmon (Oncorhynchus keta) was purified by ammonium sulfate and acetone fractionation followed by affinity chromatography, gel-filtration, and DEAE-anion exchange chromatography. The apparent molecular mass was about 24 kDa as determined by SDS-PAGE. The anionic chum salmon trypsin was moderately active toward esterase substrates such as tosyl-L-arginine methyl ester and tosyl-L-lysine methyl ester. Its amidase activity for benzoyl-L-arginine p-nitroanilide was comparative to those of bovine and Streptomyces griseus trypsins. Kinetic characteristics of anionic chum salmon, bovine, and Streptomyces griseus trypsins toward inverse substrate (p-amidinophenyl ester) were compared. Inverse substrate behaved as a specific substrate for anionic chum salmon trypsin with specific binding, efficient acylation, and relatively slow deacylation.
authors: Faculty of of Pharmaceutical Sciences, Health Sciences University of Hokkaido, Japan.
authors: H
authors: H
authors: Sekizaki
authors: K
authors: K
authors: Itoh
authors: M
authors: M
authors: Murakami
authors: E
authors: E
authors: Toyota
authors: K
authors: K
authors: Tanizawa
mesh_terms: D000577:Amides / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D000838:Anions; D001550:Benzamidines / Q000737:chemistry* / Q000378:metabolism*; D002384:Catalysis; D002417:Cattle; D004952:Esters / Q000737:chemistry* / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D015394:Molecular Structure; D017685:Oncorhynchus keta / Q000378:metabolism*; D013305:Streptomyces griseus / Q000201:enzymology; D013379:Substrate Specificity; D014357:Trypsin / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D000577:Amides; D000838:Anions; D001550:Benzamidines; D004952:Esters; C420605:amidinophenyl ester; D014357:Trypsin