Interaction of muscle glycolytic enzymes with thin filament proteins.

Purified glycolytic enzymes were individually chromatographed through columns of Sepharose 4B containing a covalently bound F-actin-tropomyosin complex. Five of these enzymes, aldolase, glyceraldehyde-phosphate dehydrogenase, lactate dehydrogenase, pyruvate kinase, and phosphoglycerate kinase were able to interact with the complex. Glucosephosphate isomerase, triosephosphate isomerase, phosphoglycerate phosphomutase, and enolase did not bind to the F-actin-tropomyosin matrix. One nonbinding enzyme, phosphoglycerate phosphomutase, was observed to interact with F-actin-tropomyosin if the column was preloaded with lactate dehydrogenase. Since at least four other glycolytic enzymes did not associate with actin directly, it is suggested that if a glycolytic enzyme complex exists, these nonadsorbing enzymes must interact with one or more of the enzymes which do bind to actin.