Characterization and purification of a Ca2+ ion-activated neutral proteinase inhibitor in rabbit skeletal muscle.
This paper describes the isolation, purification and properties of a specific inhibitor of calcium-activated neutral proteinase (CaANP) in rabbit skeletal muscle. The inhibitor was a thermo-acid-stable protein degraded by trypsin and chymotrypsin and seemed to contain two polypeptide chains with molecular weights of 70 000 and 13 000 daltons. Maximal inhibitory activity was obtained at neutral pH. High salt concentrations were needed to suppressinhibition. Inhibitor concentration had no effect on the optimal Ca++ ion levels for CaANP. These experiments also show that enzyme inhibitor association was instantaneous and did not need any incubation.
D000818:Animals; D002154:Calpain; D002848:Chromatography, DEAE-Cellulose / Q000379:methods; D002850:Chromatography, Gel / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D011480:Protease Inhibitors / Q000032:analysis / Q000302:isolation & purification*; D011817:Rabbits
D011480:Protease Inhibitors; D002154:Calpain