Douvas, Angeline S. and Harrington, Christina A. and Bonner, James (1975) Major Nonhistone Proteins of Rat Liver Chromatin: Preliminary Identification of Myosin, Actin, Tubulin, and Tropomyosin. Proceedings of the National Academy of Sciences of the United States of America, 72 (10). pp. 3902-3906. ISSN 0027-8424 http://resolver.caltech.edu/CaltechAUTHORS:DOUpnas75
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Two major nonhistone polypeptides from rat liver chromatin have been identified as myosin and actin. Preliminary observations indicate that three other chromatin polypeptides of molecular weights 50,000, 34,000, and 32,000 are tubulin and heavy and light tropomyosin, respectively. A sixth component of molecular weight 65,000 which has been purified and electrophoreses as a single band on sodium dodecyl sulfate-polyacrylamide gels may be composed in part of protease-digested myosin. These six polypeptides together account for as much as 38% of the nonhistone protein mass of chromatin in this tissue.
|Additional Information:||Copyright © 1975 by the National Academy of Sciences Contributed by James Bonner, July 17, 1975 We wish to thank Dr. Krikor Seraydarian of the University of California at Los Angeles School of Medicine for his generous gift of muscle myosin and helpful discussions, Dr. Wallace Le Stourgeon for sharing his observations on Physarum chromatin, and Dr. David Sadava for review of this manuscript. This work was supported in part by the U.S. Public Health Service (Grant GM 13762) and by a U.S. Public Health Service postdoctoral fellowship to A.S.D. A preliminary account of this work has already appeared (28).|
|Subject Keywords:||contractile proteins; endogenous protease digestion of chromatin|
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|Deposited By:||Archive Administrator|
|Deposited On:||03 Nov 2006|
|Last Modified:||26 Dec 2012 09:15|
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