Open AccessAssociation of rabbit muscle glycolytic enzymes with filamentous actin
Author(s) -
WESTRIN Hjalmar,
BACKMAN Lars
Publication year - 1983
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1983.tb07757.x
Subject(s) - actin , glycolysis , enzyme , biochemistry , actina , chemistry , biophysics , ionic strength , dextran , biology , aqueous solution , cytoskeleton , cell
The association between purified glycolytic enzymes and filamentous actin from rabbit muscle has been studied by counter‐current distribution. The co‐distribution of a glycolytic enzyme and filamentous actin leads to a significant change in the counter‐current distribution profile of the enzyme whereas that of actin is unaffected. The changes in the distribution profiles clearly demonstrated that all glycolytic enzymes studied, though to different extents, bind to filamentous actin. The aqueous two‐phase system used for the studies contained dextran, poly(ethyleneglycol) and 150 millimolal potassium phosphate buffer, pH 7.0. Since the ionic strength of the two‐phase system is determined mainly by the buffer, the glycolytic enzymes are evidently able to associate with filamentous actin, at least in the presence of neutral polymers, at ionic strengths comparable to or higher than those assumed to prevail in vivo .