Calpain II-like proteinase of scallop (Patinopecten yessoensis) striated adductor muscle.
1. A Ca(2+)-dependent cysteine proteinase was purified from scallop striated adductor muscle by ammonium sulfate fractionation and column chromatography on DEAE-cellulose and Sephacryl S-300. 2. The enzyme is of Mr approximately 200,000, composed of two Mr 100,000 subunits. 3. The enzyme is a cysteine proteinase with optimum activity at pH 6.8 and about 18 degrees C. In addition, it requires 1.7 mM Ca2+ for half-maximal activity and more than 10 mM Ca2+ for maximal activity. Thus the enzyme can be classified as calpain II.
Maeda
O
O
Department of Fisheries Chemistry, Faculty of Fisheries, Hokkaido University, Japan.
Ojima
T
T
Nishita
K
K
D000818:Animals; D002154:Calpain / Q000737:chemistry / Q000302:isolation & purification*; D002412:Cations; D003445:Crustacea / Q000201:enzymology*; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology; D011487:Protein Conformation
D002412:Cations; D002154:Calpain; D003546:Cysteine Endopeptidases