Open AccessIsolation and Structural Properties of a High‐Molecular‐Weight Actin‐Binding Protein (Filamin‐Like Protein) in Hog Thyroid Gland
Author(s) -
ROUSTAN Claude,
BOYER Mireille,
FATTOUM Abdellatif,
JEANNEAU René,
BENYAMIN Yves,
ROGER Michel,
PRADEL LouiseAnne
Publication year - 1982
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1982.tb07033.x
Subject(s) - filamin , ultracentrifuge , actin , actin binding protein , chemistry , molecular mass , size exclusion chromatography , monomer , biochemistry , cytoskeleton , actin cytoskeleton , polymer , enzyme , cell , organic chemistry
A high‐molecular‐weight protein has been isolated from hog thyroid gland. This protein, with a molecular weight of 475000 determined by ultracentrifugation and gel filtration, is a complex of two polypeptides with apparent molecular weights of 250000 and 240000. It may be related to filamin‐like proteins by its physicochemical properties and its immunogenic cross‐reactivity towards gizzard filamin antibodies. Furthermore it interacts with F‐actin in a stoichiometry of 1 mol of high‐molecular‐weight protein/∼ 12–14 mol actin monomer allowing microfilament association, as shown by electron microscopy.