Bovine lens multicatalytic proteinase complex

Enzyme Protein. 1993;47(4-6):202-9. doi: 10.1159/000468679.

Abstract

The ocular lens grows by laying down new cells on top of old in a differentiation process that results in loss of protein-synthesizing capacity, but preservation of the cells themselves for the lifetime of the organism. The transparency and refractive index of the lens depend on protein integrity and longevity, yet proteolysis is needed for normal growth and development. Therefore, control of proteolysis must be stringent. Here we review the structural features and major proteolytic enzymes of the lens and the properties of the bovine lens multicatalytic proteinase complex, including native and SDS-PAGE patterns, and activation and inhibition by cations, amphiphilic molecules and temperature.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cations / pharmacology
  • Cattle
  • Cysteine Endopeptidases / metabolism*
  • Enzyme Activation
  • Hot Temperature
  • In Vitro Techniques
  • Lens, Crystalline / enzymology*
  • Lens, Crystalline / growth & development
  • Molecular Sequence Data
  • Multienzyme Complexes / metabolism*
  • Oligopeptides / chemistry
  • Proteasome Endopeptidase Complex
  • Substrate Specificity

Substances

  • Cations
  • Multienzyme Complexes
  • Oligopeptides
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex