Rogovskiĭ S P, Mel'nichuk D A, Koval'chuk I A
Ukr Biokhim Zh (1978). 1988 Mar-Apr;60(2):81-5.
The method of fluorescent titration was used to study the effect of carbonic acid on the process of NADH binding with the purified preparation of glutamate dehydrogenase as well as on fluorescent properties of the above mentioned coenzyme. It is shown that in bicarbonate buffer at the alkaline values of pH there is a decrease in the maximal capacity of the binding sites of the enzyme with low affinity to co-enzyme. The capacity of high-affinity binding sites in this case is unchanged. It is found that pCO2, HCO3- and H+ exert an effect on the dissociation constants of the NADH-glutamate dehydrogenase complex as well as on fluorescent properties of bound NADH. It is supposed that the effects observed are a result of the interaction of dissolved carbon dioxide with free amino groups of protein molecule.
采用荧光滴定法研究了碳酸对NADH与纯化的谷氨酸脱氢酶制剂结合过程以及上述辅酶荧光特性的影响。结果表明，在pH呈碱性的碳酸氢盐缓冲液中，酶与辅酶亲和力较低的结合位点的最大容量降低。此时高亲和力结合位点的容量不变。研究发现，pCO₂、HCO₃⁻和H⁺对NADH - 谷氨酸脱氢酶复合物的解离常数以及结合的NADH的荧光特性均有影响。据推测，观察到的这些效应是溶解的二氧化碳与蛋白质分子的游离氨基相互作用的结果。
