Autolytic activation of calcium-activated neutral protease

Biochem Biophys Res Commun. 1986 Jul 31;138(2):638-43. doi: 10.1016/s0006-291x(86)80544-7.

Abstract

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.

MeSH terms

  • Animals
  • Calpain / metabolism*
  • Enzyme Activation
  • Kinetics
  • Macromolecular Substances
  • Molecular Weight
  • Muscles / enzymology*
  • Rabbits
  • Vimentin / metabolism

Substances

  • Macromolecular Substances
  • Vimentin
  • Calpain