Purification and properties of a novel latent proteinase showing myosin heavy chain-degrading activity from threadfin-bream muscle.
A novel latent proteinase of which activity was induced by heating in the presence of NaCl was purified to homogeneity from threadfin-bream muscle by a combination of DEAE-cellulose, Con A-Sepharose, Arg-Sepharose, and Shim-pack HAC chromatographies. This proteinase was a glycoprotein having a monomeric subunit structure; Mr was estimated to be 77,000 on SDS-PAGE analysis. The proteinase hydrolyzed Boc-Leu-Thr-Arg-MCA as well as myosin heavy chain in the presence of 2-4% NaCl at pH 7.0 and at 60 degrees C, optimally. The proteinase was classified as serine proteinase based on the effects of soybean trypsin inhibitor, leupeptin, and antipain.
Kinoshita
M
M
Department of Fisheries, Faculty of Agriculture, Kyoto University.
Toyohara
H
H
Shimizu
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D005399:Fishes / Q000378:metabolism*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D009132:Muscles / Q000187:drug effects / Q000201:enzymology*; D009218:Myosins / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000032:analysis*; D012965:Sodium Chloride / Q000494:pharmacology; D013379:Substrate Specificity; D013696:Temperature
D012965:Sodium Chloride; D012697:Serine Endopeptidases; D009218:Myosins