Purification and characterization of a calcium-dependent protease from rat liver.
A calcium-dependent protease, previously identified in rat liver and designated peak II [DeMartino, G. N. (1981) Arch. Biochem. Biophys. 211, 253-257], was purified and characterized. The calcium-dependent proteolytic activity was accounted for by an 80 000-dalton protein. Depending on the method of purification, we found that this protease could be associated with a 28 000-dalton subunit, which was devoid of protease activity. The catalytic characteristics of the two different forms of the protease were indistinguishable. Each was half-maximally activated by approximately 250 microM calcium.
D000818:Animals; D002154:Calpain; D002847:Chromatography, Agarose; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D011487:Protein Conformation; D051381:Rats
D010450:Endopeptidases; D002154:Calpain