Mel'nuchuk D A, Rogovskiĭ S P, Koval'chuk I A
Ukr Biokhim Zh (1978). 1985 Nov-Dec;57(6):46-51.
Different levels of carbon dioxide (10,20, 40, 80, mM) at pH 6.7, 7.3, 7.6 and 8.5 of incubation media were studied for their effect on the intensity of binding of 14C from bicarbonate buffer by crystalline NAD(P)+-dependent glutamate dehydrogenase from the bovine liver. The effect of a variety of substrates and effectors on this process is investigated. The intensity of the radioactive label binding is shown to increase with pH of the incubation medium and carbon dioxide concentration in it. When acidifying the medium (up to pH 6.5) the enzyme under study does not bind 14C. The preincubation of the enzyme with pyridoxal-5-phosphate decreases considerably the intensity of the label binding with the protein. On the basis of these data a conclusion is drawn about the interaction of CO2 with free amino groups of the enzyme molecule by the type of the carbamate formation. GTP and NADH inhibit this process as well.
研究了在pH值为6.7、7.3、7.6和8.5的孵育介质中，不同水平的二氧化碳（10、20、40、80 mM）对牛肝中结晶NAD(P)+依赖性谷氨酸脱氢酶从碳酸氢盐缓冲液中结合14C强度的影响。研究了多种底物和效应物对该过程的影响。放射性标记结合强度显示随着孵育介质的pH值及其二氧化碳浓度的增加而增加。当将介质酸化至pH 6.5时，所研究的酶不结合14C。用磷酸吡哆醛对酶进行预孵育会显著降低标记与蛋白质的结合强度。基于这些数据，得出关于二氧化碳与酶分子游离氨基通过氨基甲酸盐形成类型相互作用的结论。GTP和NADH也抑制该过程。
