Major nonhistone proteins of rat liver chromatin: preliminary identification of myosin, actin, tubulin, and tropomyosin.
AUTOR(ES)
Douvas, A S
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=433104Documentos Relacionados
- In vitro synthesis of native myosin, actin, and tropomyosin from embryonic chick polyribosomes.
- Immunocytochemical localization of tubulin, actin, and myosin in axonemes of ciliated cells from quail oviduct.
- Interactions of actin, myosin, and an actin-binding protein of chronic myelogenous leukemia leukocytes.
- Identification of nonhistone chromatin proteins in chromatin subunits.
- Conformational change and cooperativity in actin filaments free of tropomyosin.