Zimin Iu V, Solopaeva I M
Biull Eksp Biol Med. 1992 Jul;114(8):217-8.
The purpose of this report is to demonstrate that chorionic gonadotropin (CG) interacts nonspecifically with lactate dehydrogenase changing its catalytic activity. The binding in vitro of CG (5 mg/ml) to the enzyme is accompanied by conformational changes of its protein and kinetic characteristics. It may be possible that chorionic gonadotropin exercises a controlling influence on lactate dehydrogenase activity in the cell.
本报告的目的是证明绒毛膜促性腺激素（CG）与乳酸脱氢酶非特异性相互作用，从而改变其催化活性。CG（5毫克/毫升）与该酶的体外结合伴随着其蛋白质构象变化和动力学特征改变。绒毛膜促性腺激素可能对细胞中的乳酸脱氢酶活性发挥调控作用。
