Binding of actin to lens alpha crystallins
作者:
GopalakrishnanS.,
TakemotoL.,
期刊:
Current Eye Research
(Taylor Available online 1992)
卷期:
Volume 11,
issue 9
页码: 929-933
ISSN:0271-3683
年代: 1992
DOI:10.3109/02713689209033490
出版商: Taylor&Francis
数据来源: Taylor
摘要:
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.
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