Burlakova A A, Kurganov B I, Chebotareva N A, Debabov V G
State Research Institute of Genetics and Selection of Industrial Microorganisms, Moscow Bakh Institute of Biochemistry, Russian Academy of Sciences, Russia.
Membr Cell Biol. 1997;10(5):543-51.
The catalytic activity of uridine phosphorylase from Escherichia coli K-12 entrapped in hydrated reversed micelles of aerosol OT (AOT) in octane has been studied as a function of the degree of hydration of the micelles. It was shown that the catalytic activity of uridine phosphorylase reached maximum values at [H2O/[AOT] ratios equal to 8.4, 12.9, 16.1 and 18.6. Based on the sedimentation data the conclusion has been made that the maxima of the catalytic activity correspond to the monomeric, dimeric, trimeric and tetrameric forms of the enzyme. The measurements of the rate of the enzymatic reaction catalyzed by uridine phosphorylase entrapped in hydrated reversed micelles at various concentrations of AOT indicate that the monomeric enzyme form, in contrast to the trimeric and tetrameric forms, exhibits the membranotropic properties.
对包裹于辛烷中气溶胶OT（AOT）的水合反相胶束中的大肠杆菌K - 12尿苷磷酸化酶的催化活性，作为胶束水合程度的函数进行了研究。结果表明，尿苷磷酸化酶的催化活性在水与AOT的比例等于8.4、12.9、16.1和18.6时达到最大值。基于沉降数据得出结论，催化活性的最大值对应于该酶的单体、二聚体、三聚体和四聚体形式。对包裹于不同浓度AOT的水合反相胶束中的尿苷磷酸化酶所催化的酶促反应速率的测量表明，与三聚体和四聚体形式相比，单体酶形式表现出膜亲和特性。
