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.
D000199:Actins / Q000378:metabolism*; D000818:Animals; D002846:Chromatography, Affinity; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism; D006019:Glycolysis; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D009132:Muscles / Q000201:enzymology*; D010735:Phosphoglycerate Kinase / Q000378:metabolism; D011770:Pyruvate Kinase / Q000378:metabolism; D011817:Rabbits; D014335:Tropomyosin / Q000378:metabolism*
D000199:Actins; D014335:Tropomyosin; D007770:L-Lactate Dehydrogenase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D011770:Pyruvate Kinase; D010735:Phosphoglycerate Kinase; D005634:Fructose-Bisphosphate Aldolase