Alpha-crystallin, a molecular chaperone, forms a stable complex with carbonic anhydrase upon heat denaturation.

Published

Journal Article

Alpha-crystallin, a major eye lens protein of vertebrates has been characterized as a molecular chaperone based on its ability to inhibit the aggregation of proteins undergoing thermal denaturation (Horwitz, J., Proc. Natl. Acad. Sci. USA 1992, 89, 10449-10453). To understand the mechanisms underlying this chaperone-like activity, the present study addressed molecular interactions between alpha-crystallin and its target proteins. Using carbonic anhydrase as a model target protein, we demonstrate complex formation between the 2 proteins upon heating, as assessed by the criteria of agarose gel electrophoresis, immunoprecipitation, ultrafiltration and gel filtration chromatography. The complex of alpha-crystallin and carbonic anhydrase is stable, at room temperature and at 4 degrees C, for over 18 hours, and is non-covalent in nature. The results also indicate that alpha-crystallin binds the early non-native form of the target protein.

Full Text

Duke Authors

Cited Authors

  • Rao, PV; Horwitz, J; Zigler, JS

Published Date

  • February 15, 1993

Published In

Volume / Issue

  • 190 / 3

Start / End Page

  • 786 - 793

PubMed ID

  • 8094957

Pubmed Central ID

  • 8094957

International Standard Serial Number (ISSN)

  • 0006-291X

Digital Object Identifier (DOI)

  • 10.1006/bbrc.1993.1118

Language

  • eng

Conference Location

  • United States