Lens alpha-crystallin: chaperone-like properties

Methods Enzymol. 1998:290:365-83. doi: 10.1016/s0076-6879(98)90032-5.
No abstract available

Publication types

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

MeSH terms

  • Alcohol Dehydrogenase / metabolism
  • Animals
  • Cattle
  • Circular Dichroism
  • Cloning, Molecular
  • Crystallins / chemistry*
  • Crystallins / metabolism
  • Disulfides / metabolism
  • Heat-Shock Proteins / chemistry
  • Insulin / metabolism
  • Lactalbumin / metabolism
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / metabolism*
  • Protein Binding / physiology
  • Protein Denaturation
  • Protein Folding
  • Recombinant Proteins / chemistry

Substances

  • Crystallins
  • Disulfides
  • Heat-Shock Proteins
  • Insulin
  • Molecular Chaperones
  • Recombinant Proteins
  • Lactalbumin
  • Alcohol Dehydrogenase