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  • 1
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    Localization of the chaperone binding site (1993)
    In:  Other Sources
    Details
    Publication Date: 2011-08-24
    Description: The hypothesis derived from models of the multi-oligomeric chaperone complex suggests that partially denatured proteins bind in a central cavity in the aggregate. To test this hypothesis, the molecular chaperone, alpha crystallin, was bound to partially denatured forms of gamma crystallin, and the binding site was visualized by immunogold localization. In an alternative approach, gold particles were directly complexed with gamma crystallin, followed by binding to the alpha crystallin aggregate. In both cases, binding was localized to the central region of the aggregate, confirming for the first time that partially denatured proteins do indeed bind to a central region of the molecular chaperone aggregate.
    Keywords: Life Sciences (General)
    Type: Biochemical and biophysical research communications (ISSN 0006-291X); Volume 192; 3; 1147-54
    Format: text
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    NASA TECHNICAL REPORTS
  • 2
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    Association of actin with alpha crystallins (1993)
    In:  Other Sources
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    Publication Date: 2011-08-24
    Description: The alpha crystallins are cytosolic proteins that co-localize and co-purify with actin-containing microfilaments. Affinity column chromatography employing both covalently-coupled actin or alpha crystallin was used to demonstrate specific and saturable binding of actin with alpha crystallin. This conclusion was confirmed by direct visualization of alpha aggregates bound to actin polymerized in vitro. The significance of this interaction in relation to the functional properties of these two polypeptides will be discussed.
    Keywords: Life Sciences (General)
    Type: Transactions of the Kansas Academy of Science (ISSN 0022-8443); Volume 96; 1-2; 7-12
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    NASA TECHNICAL REPORTS
  • 3
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    Binding of actin to lens alpha crystallins (1992)
    In:  Other Sources
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    Publication Date: 2011-08-24
    Description: Actin has been coupled to a cyanogen bromide-activated Sepharose 4B column, then tested for binding to alpha, beta, and gamma crystallin preparations from the bovine lens. Alpha, but not beta or gamma, crystallins bound to the actin affinity column in a time dependent and saturable manner. Subfractionation of the alpha crystallin preparation into the alpha-A and alpha-B species, followed by incubation with the affinity column, demonstrated that both species bound approximately the same. Together, these studies demonstrate a specific and saturable binding of lens alpha-A and alpha-B with actin.
    Keywords: Life Sciences (General)
    Type: Current eye research (ISSN 0271-3683); Volume 11; 9; 929-33
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    NASA TECHNICAL REPORTS
  • 4
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    Alpha-A crystallin: quantitation of C-terminal modification during lens aging (1994)
    In:  Other Sources
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    Publication Date: 2011-08-24
    Description: Previous studies have demonstrated that the C-terminal region of alpha-A crystallin is susceptible to age-dependent, posttranslational modification. To quantitate the amount of modification, alpha-A crystallin was purified from total proteins of the aging bovine lens, then digested with lys-C endoproteinase. Reverse phase, high pressure liquid chromatography was used to resolve and quantitate the resulting peptides, to determine the amount of C-terminal peptide relative to peptides from other regions of the protein that have not been reported to undergo modification. The results indicate that relative to alpha-A crystallin from newborn lens, posttranslational modification has occurred in approximately 45-55% of the C-terminal region from mature lens. These results demonstrate extensive modification of the C-terminal region of alpha-A crystallin from the mature lens, indicating that during the aging process, posttranslational modifications in this region may make significant contributions to the aggregated state and/or molecular chaperone properties of the molecule.
    Keywords: Life Sciences (General)
    Type: Current eye research (ISSN 0271-3683); Volume 13; 12; 879-83
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    NASA TECHNICAL REPORTS
  • 5
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    An assay for intermolecular exchange of alpha crystallin (1992)
    In:  Other Sources
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    Publication Date: 2011-08-24
    Description: 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.
    Keywords: Life Sciences (General)
    Type: Investigative ophthalmology & visual science (ISSN 0146-0404); Volume 33; 10; 2936-41
    Format: text
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    NASA TECHNICAL REPORTS
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