反胶束中的蛋白质-蛋白质相互作用：在异辛烷中双（2-乙基己基）磺基琥珀酸钠（AOT）的反胶束中，胰蛋白酶对蛋白质底物α-胰凝乳蛋白酶原A表现出超活性。
Protein-protein interactions in reverse micelles: trypsin shows superactivity towards a protein substrate alpha-chymotrypsinogen A in reverse micelles of sodium bis(2-ethylhexyl)sulfosuccinate (AOT) in isooctane.
作者信息
Fadnavis N W, Chandraprakash Y, Deshpande A
机构信息
Organic Division-II, Indian Institute of Chemical Technology, Hyderabad.
出版信息
Biochimie. 1993;75(11):995-9. doi: 10.1016/0300-9084(93)90151-h.
Protein-protein interactions in reverse micelles of sodium bis(2-ethylhexyl)sulfosuccinate (AOT), in isooctane containing varying amounts of Tris buffer are studied by using activation of alpha-chymotrypsinogen A by trypsin (EC 3.4.21.4) to alpha-chymotrypsin (EC 3.4.21.1) as a model reaction. It has been found that protein-protein interactions are strongly dependent on the water content of the medium. At an optimum water content the activation reaction in reverse micelles is faster than reaction in water by a factor of 21.3. At lower water content both reaction rates and the conversion of alpha-chymotrypsinogen A into alpha-chymotrypsin decrease with decrease in water content of the reaction medium.
通过以胰蛋白酶（EC 3.4.21.4）将α-胰凝乳蛋白酶原A激活为α-胰凝乳蛋白酶（EC 3.4.21.1）作为模型反应，研究了在含有不同量Tris缓冲液的异辛烷中，双（2-乙基己基）磺基琥珀酸钠（AOT）反胶束中的蛋白质-蛋白质相互作用。已发现蛋白质-蛋白质相互作用强烈依赖于介质的水含量。在最佳水含量下，反胶束中的激活反应比在水中的反应快21.3倍。在较低水含量下，反应速率以及α-胰凝乳蛋白酶原A向α-胰凝乳蛋白酶的转化率均随反应介质水含量的降低而降低。
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