Autolytic activation of calcium-activated neutral protease.
Degradation of vimentin by native low calcium ion-requiring protease (mu CANP) was compared to that by autodigested mu CANP. On activation with 5 mM barium ions, a lag time was observed for the case of native mu CANP. This provides direct evidence that native mu CANP is inactive as a protease and must be autolyzed to be activated. Most of the protease activity can be accounted for by autodigested mu CANP with a 76 K polypeptide but another species with 50 K polypeptide may also be active.
D000818:Animals; D002154:Calpain / Q000378:metabolism*; D004789:Enzyme Activation; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D011817:Rabbits; D014746:Vimentin / Q000378:metabolism
D046911:Macromolecular Substances; D014746:Vimentin; D002154:Calpain