Alpha-crystallin-Crystallin, a Molecular Chaperone, Forms a Stable Complex with Carbonic Anhydrase upon Heat Denaturation

P. Vasantha Rao, Joseph Horwitz, Samuel Zigler

Research output: Contribution to journalArticlepeer-review

105 Scopus citations


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 α-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 α-crystallin and carbonic anhydrase is stable, at room temperature and at 4°C, for over 18 hours, and is non-covalent in nature. The results also indicate that α-crystallin binds the early non-native form of the target protein.

Original languageEnglish (US)
Pages (from-to)786-793
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Jan 1 1993

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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