Everse J, Berger R L, Kaplan N O
Science. 1970 Jun 5;168(3936):1236-8. doi: 10.1126/science.168.3936.1236.
Lactate dehydrogenases at physiological concentrations are inhibited by high concentrations of pyruvate when the enzyme and the pyruvate are incubated in the presence of oxidized nicotinamide-adenine dinucleotide before assay. The inhibition is much more pronounced with the H-type than with the M-type lactate dehydrogenase. These results suggest that substrate inhibition may be operative in vivo.
当在测定前将酶和丙酮酸在氧化型烟酰胺腺嘌呤二核苷酸存在的情况下孵育时,生理浓度的乳酸脱氢酶会受到高浓度丙酮酸的抑制。与M型乳酸脱氢酶相比,H型乳酸脱氢酶的抑制作用更为明显。这些结果表明底物抑制可能在体内起作用。