偶联酶促反应在肌原a蛋白晶体中测量。

T Keleti, R Berni, M Vas, A Mozzarelli, G L Rossi
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引用次数: 0

摘要

在聚乙二醇存在下,用显微分光光度法测定了肌原A单晶中果糖-1,6-二磷酸醛缩酶与sn-甘油-3-磷酸脱氢酶、3-磷酸甘油激酶与d -甘油醛-3-磷酸脱氢酶、三磷酸异构酶和sn-甘油-3-磷酸脱氢酶的成对偶联反应。用偏振光进行的显微分光光度测量表明,蛋白质分子是定向的,NADH以确定的定向与晶体内的脱氢酶结合。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Coupled enzymatic reactions measured in a single protein crystal from myogen A.

Pairwise coupled reactions of fructose-1,6-bisphosphate aldolase and sn-glycerol-3-phosphate dehydrogenase, 3-phosphoglycerate kinase and D-glyceraldehyde-3-phosphate dehydrogenase, triosephosphate isomerase and sn-glycerol-3-phosphate dehydrogenase have been detected by microspectrophotometry in single crystals obtained from myogen A in the presence of polyethylene glycol. Microspectrophotometric measurements with polarized light demonstrate that the protein molecules are oriented and that NADH is bound with a definite orientation to the dehydrogenases within the crystal.

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