Kinetic analysis of lactate dehydrogenase using integrated rate equations.
The reaction catalyzed by lactate dehydrogenase was analyzed under fully second-order conditions using integrated rate equations. A two-step regression analysis was utilized to fit twenty-one progress curves repeated in sextuplicate to the general mechanism second-order integrated rate equation with additional terms of substrate inhibition. The fitting error was less than one percent. The resulting kinetic constants support a ternary complex mechanism; in no case were constants supporting another mechanism predicted. The inhibition constant for oxamate was also determined.
Holmes
L D
LD
Department of Chemistry and Biochemistry, Utah State University, Logan 84322.
Schiller
M R
MR
Boeker
E A
EA
D000818:Animals; D001667:Binding, Competitive; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D008433:Mathematics; D009243:NAD / Q000378:metabolism; D011773:Pyruvates / Q000378:metabolism; D019289:Pyruvic Acid; D011817:Rabbits; D012044:Regression Analysis; D012710:Serum Albumin, Bovine / Q000494:pharmacology
D007527:Isoenzymes; D011773:Pyruvates; D009243:NAD; D012710:Serum Albumin, Bovine; D019289:Pyruvic Acid; D007770:L-Lactate Dehydrogenase