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