Equilibrium partition studies of the myofibrillar interactions of glycolytic enzymes.
The interactions of several glycolytic enzymes with muscle myofibrils in imidazole-chloride buffer (pH 6.8, I 0.158) have been investigated by equilibrium partition studies. Results for aldolase, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase, and phosphofructokinase are interpreted in terms of a myofibrillar capacity of 76 nmol/g protein and a single intrinsic association constant for each tetravalent enzyme with matrix sites. The existence of separate myofibrillar sites for aldolase and glyceraldehyde-3-phosphate dehydrogenase is established by demonstrating independence of the binding of each enzyme upon the presence of the other. Although this investigation provides further physicochemical support for myofibrillar adsorption of glycolytic enzymes in the cellular environment, its findings are incompatible with the proposition (B. I. Kurganov, N. P. Sugrobova, and L. S. Mil'man (1985) J. Theor. Biol. 116, 509-526) that the phenomenon reflects the formation of a specific multienzyme complex attached to the myofibril.
Harris
S J
SJ
Department of Biochemistry, University of Queensland, St. Lucia, Australia.
Winzor
D J
DJ
D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000494:pharmacology; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D006019:Glycolysis; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D008433:Mathematics; D009132:Muscles / Q000201:enzymology*; D009210:Myofibrils / Q000378:metabolism*; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D011485:Protein Binding; D011817:Rabbits
D007770:L-Lactate Dehydrogenase; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D010732:Phosphofructokinase-1; D005634:Fructose-Bisphosphate Aldolase; D002118:Calcium