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Binding of actin to lens alpha crystallinsActin 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.
Document ID
20050000613
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: Current eye research
Volume: 11
Issue: 9
ISSN: 0271-3683
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Other
Keywords
NASA Discipline Cell Biology
Non-NASA Center