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Alpha-A crystallin: quantitation of C-terminal modification during lens agingPrevious 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.
Document ID
20050000283
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Takemoto, L.
(Kansas State University Manhattan 66506)
Gopalakrishnan, S.
Spooner, B. S.
Date Acquired
August 22, 2013
Publication Date
December 1, 1994
Publication Information
Publication: Current eye research
Volume: 13
Issue: 12
ISSN: 0271-3683
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other
Keywords
NASA Discipline Cell Biology
Non-NASA Center

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