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Characterization of the major cyanogen bromide fragment of alpha-A crystallinAlpha crystallin from the bovine lens has been digested with cyanogen bromide, and the major fragment (CB-1) has been purified using reverse phase HPLC. Characterization of this fragment by Edman degradation and antisera to synthetic peptides indicates that it originates from alpha-A crystallin, but lacks the N-terminal methionine and the last 35 amino acids from the C-terminus of the molecule. The purified CB-1 fragment binds as well as native alpha crystallin to lens membrane, but is unable to self-assemble into the correct size of high molecular weight oligomeric complexes characteristic of the intact alpha-A chain. Together, these results demonstrate that the alpha-A chain is comprised of at least two functional domains, one of which is involved in binding of alpha-A crystallin to lens membrane, and another which is necessary for correct self-assembly of the molecule into high molecular weight oligomers.
Document ID
20050000846
Acquisition Source
Legacy CDMS
Document Type
Reprint (Version printed in journal)
Authors
Ifeanyi, F.
(Kansas State University Manhattan 66506)
Takemoto, L.
Spooner, B. S.
Date Acquired
August 22, 2013
Publication Date
June 1, 1991
Publication Information
Publication: Current eye research
Volume: 10
Issue: 6
ISSN: 0271-3683
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other
Keywords
Non-NASA Center
NASA Discipline Cell Biology

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