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An assay for intermolecular exchange of alpha crystallinAn 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.
Document ID
20050000610
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Gopalakrishnan, S.
(Kansas State University Manhattan 66506)
Takemoto, L.
Spooner, B. S.
Date Acquired
August 22, 2013
Publication Date
September 1, 1992
Publication Information
Publication: Investigative ophthalmology & visual science
Volume: 33
Issue: 10
ISSN: 0146-0404
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other
Keywords
NASA Discipline Cell Biology
Non-NASA Center

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