Interaction of muscle glycolytic enzymes with thin filament proteins

Abstract

Purified glycolytic enzymes were individually chromatographed through columns of Sepharose 4B containing a covalently bound F-actin-tropomyosin complex from rabbit skeletal muscle. 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 4 other glycolytic enzymes did not associate with actin directly, if a glycolytic complex exists, these nonadsorbing enzymes must interact with 1 or more of the enzymes which do bind to actin.