September 1992
Volume 33, Issue 10
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Articles  |   September 1992
An assay for intermolecular exchange of alpha crystallin.
Author Affiliations
  • S Gopalakrishnan
    Division of Biology, Kansas State University, Manhattan 66506.
  • L Takemoto
    Division of Biology, Kansas State University, Manhattan 66506.
Investigative Ophthalmology & Visual Science September 1992, Vol.33, 2936-2941. doi:
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      S Gopalakrishnan, L Takemoto; An assay for intermolecular exchange of alpha crystallin.. Invest. Ophthalmol. Vis. Sci. 1992;33(10):2936-2941.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

An affinity column of alpha crystallin linked to cyanogen bromide-activated Sepharose was developed to study the exchange of alpha subunits. Alpha crystallin bound to the Sepharose-alpha complex was dissociated with 8 mol/l urea, followed by quantitation using high-performance reverse-phase liquid chromatography. The time course of binding at 37 degrees C showed a hyperbolic binding pattern reaching equilibrium between 6-18 hr. Under these conditions, binding of beta and gamma crystallins to the same matrix was less than 10% of the alpha values, as was binding of alpha to glycine-coupled Sepharose. This assay was used to demonstrate changes in the subunit exchange of alpha crystallins present in high molecular weight versus lower molecular weight aggregates of the human lens. These results show that this binding procedure was a specific reproducible assay that might be used to study intermolecular interactions of the alpha crystallins.

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