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Record 88 of 2744
An assay for intermolecular exchange of alpha crystallin
Author and Affiliation:
Gopalakrishnan, S.(Kansas State University, Division of Biology, Manhattan 66506)
Takemoto, L.
Spooner, B. S. [Principal Investigator]
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.
Publication Date: Sep 01, 1992
Document ID:
20050000610
(Acquired Jan 06, 2005)
Subject Category: LIFE SCIENCES (GENERAL)
Document Type: Journal Article
Publication Information: Investigative ophthalmology & visual science (ISSN 0146-0404); Volume 33; 10; 2936-41
Publisher Information: United States
Description: In English
Distribution Limits: Unclassified; Publicly available; Unlimited
Rights: Copyright
NASA Terms: ASSAYING; EYE (ANATOMY); CATTLE; LIQUID CHROMATOGRAPHY
Other Descriptors: CRYSTALLINS/METABOLISM; LENS, CRYSTALLINE/METABOLISM; ANIMALS; CATTLE; CHROMATOGRAPHY, AFFINITY; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; HUMAN; SEPHAROSE/CHEMISTRY; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, NON-P.H.S; SUPPORT, U.S. GOV'T, P.H.S; NASA DISCIPLINE CELL BIOLOGY; NON-NASA CENTER
Availability Source: Other Sources
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