Purification and some properties of a trypsin inhibitor from carp (Cyprinus carpio) muscle.
A trypsin inhibitor was purified from carp muscle to apparent homogeneity by the successive chromatographies of DEAE-cellulose, DEAE-Sepharose CL-6B, Con A-Sepharose, Ultrogel AcA 44 and hydroxylapatite. The mol. wt of the inhibitor was estimated to be 58,000 by SDS-polyacrylamide gel electrophoresis or 50,000 by gel filtration. The inhibitor seemed to form a 1:1 stoichiometric complex with trypsin, alpha-chymotrypsin and elastase, respectively. Carp muscle trypsin inhibitor was likely to be identical with serum alpha 1-proteinase inhibitor judging from its glycoprotein nature, mol. wt and the inhibition stoichiometry.
D000818:Animals; D002347:Carps; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D007700:Kinetics; D008970:Molecular Weight; D009132:Muscles / Q000032:analysis*; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D014357:Trypsin / Q000378:metabolism; D014361:Trypsin Inhibitors / Q000302:isolation & purification* / Q000494:pharmacology
D014361:Trypsin Inhibitors; D002918:Chymotrypsin; D010196:Pancreatic Elastase; D014357:Trypsin