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Curr Eye Res. 1992 Sep;11(9):929-33.

Binding of actin to lens alpha crystallins.

Author information

1
Division of Biology, Kansas State University, Manhattan 66506.
2
KS St U, Manhattan

Abstract

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.

PMID:
1424733
DOI:
10.3109/02713689209033490
[Indexed for MEDLINE]

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