Rao S V, Indira K
Department of Zoology, Sri Venkateswara University, Tirupati, India.
Biochem Mol Biol Int. 1993 Jan;29(1):63-7.
Guanidine-induced alterations in substrate-dependent kinetics of glycine amidinotransferase (GAT) have been investigated in homogenates of rat kidney. Guanidine hydrochloride (GuHCl) induced a mixed type of inhibition by decreasing the maximal velocity (Vmax) and increasing the Michaelis-Menten constant (Km). The finding of a value of Ki smaller than that of Ki' denoted that the inhibition of GAT may be due to decreased E to S affinity rather than to reduction in the active site density of the enzyme.
在大鼠肾脏匀浆中研究了胍诱导的甘氨酸脒基转移酶（GAT）底物依赖性动力学变化。盐酸胍（GuHCl）通过降低最大反应速度（Vmax）和增加米氏常数（Km）诱导混合型抑制。Ki值小于Ki'值的结果表明，GAT的抑制可能是由于E与S亲和力降低，而非酶活性位点密度降低所致。
