Association of rabbit muscle glycolytic enzymes with filamentous actin

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Abstract
The association between purified glycolytic enzymes and filamentous actin from rabbit muscle was studied by counter-current distribution. Thie 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 enzyme studied, though to different extents, bind to filamentous actin. The aqueous 2-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 2 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.