Premium
The Polymeric State of Actin in the Human Erythrocyte Cytoskeleton
Author(s) -
Atkinson Mark A.L.,
Morrow Jon S.,
Marchesi Vincent T.
Publication year - 1982
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.1982.240180410
Subject(s) - polymer , monomer , actin , size exclusion chromatography , phalloidin , cytoskeleton , chemistry , ionic strength , biophysics , sepharose , actin binding protein , biochemistry , actin cytoskeleton , chromatography , polymer chemistry , cell , biology , enzyme , organic chemistry , aqueous solution
Reports on the polymeric state of actin in the red cell have been diverse. We have used phalloidin to stabilize the actin in erythrocyte ghosts prior to extraction in low ionic strength media. A mild proteolytic digestion and Sepharose 4B gel filtration enable an F‐actin polymer to be isolated in pure form [1]. Detailed size analysis of this polymer in a range of experiments suggests that actin exists in the erythrocyte principally as a polymer of 100 nm length composed of 30 monomers in a double helical chain 15 monomers long with an estimated molecular weight of 1.3 × 10 6 daltons.