Association of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase and 3-phosphoglycerate kinase. The biochemical and electron-microscopic evidence.

Rabbit muscle glyceraldehyde-3-phosphate dehydrogenase covalently bound to Sepharose was shown to form a complex with soluble 3-phosphoglycerate kinase. The strength of the association appeared to depend upon the functional state of both enzymes. The holoform of the dehydrogenase exhibited a lower affinity for the kinase than the enzyme-3-phosphoglycerol.NADH complex. The substrate-free 3-phosphoglycerate kinase associated much stronger with the acylated dehydrogenase than the kinase in complex with 1,3-diphosphoglycerate. Electron-microscopic evidence for the association of the soluble acyl-glyceraldehyde-3-phosphate dehydrogenase.NADH complex and 3-phosphoglycerate kinase was also obtained.