title: Comparative studies on heat stability and autolysis of scallop (Patinopecten yessoensis) calpain II-like proteinase and rabbit calpain II.
abstract: 1. The scallop calpain-like proteinase is about five times more labile than the rabbit calpain II upon heat treatment at 35 degrees C. 2. By autolysis of the scallop proteinase of two 100 kDa subunits, 90, 45 and 30 kDa fragments were formed. Thereby the activity decreased monophasically in the presence of millimolar order of Ca2+, but did not increase in the presence of micromolar order of Ca2+ unlike the rabbit calpain II.
authors.affiliation: Department of Fisheries Chemistry, Faculty of Fisheries, Hokkaido University, Japan.
authors.forename: O
authors.initials: O
authors.lastname: Maeda
authors.forename: T
authors.initials: T
authors.lastname: Ojima
authors.forename: K
authors.initials: K
authors.lastname: Nishita
mesh_terms: D000818:Animals; D001329:Autolysis; D002154:Calpain / Q000737:chemistry*; D003445:Crustacea / Q000201:enzymology*; D003546:Cysteine Endopeptidases / Q000737:chemistry*; D004795:Enzyme Stability; D006358:Hot Temperature; D008970:Molecular Weight; D011487:Protein Conformation; D011817:Rabbits; D013045:Species Specificity
chemical_list: D002154:Calpain; D003546:Cysteine Endopeptidases