Purification and properties of carp (Cyprinus carpio) muscle calpain II (high-Ca2+-requiring form of calpain).
Calpain (Ca2+-dependent cysteine proteinase) was purified to apparent homogeneity from carp muscle by the method of DEAE-cellulose, hydroxylapatite and Ultrogel AcA 34 column chromatographies. The purified enzyme is classified as calpain II (high-Ca2+-requiring form of calpain) from the effects of Ca2+ concentration, pH and the antibiotics on the activity. Carp muscle calpain II was inhibited by rat liver calpastatin, the specific inhibitor for calpain. It is probable that the calpain-calpastatin system may play a biologically fundamental and common role in various cells, since the inhibitory effect of calpastatin on calpain from different tissues of different species is well conserved.
Toyohara
H
H
Makinodan
Y
Y
Tanaka
K
K
Ikeda
S
S
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002135:Calcium-Binding Proteins / Q000494:pharmacology; D002154:Calpain; D002347:Carps; D002413:Cations, Divalent; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000378:metabolism; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D011480:Protease Inhibitors / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains
D002135:Calcium-Binding Proteins; D002413:Cations, Divalent; D011480:Protease Inhibitors; C033668:calpastatin; D010450:Endopeptidases; D002154:Calpain; D002118:Calcium