在粗糙脉孢菌谷氨酸脱氢酶中，还原型烟酰胺腺嘌呤二核苷酸磷酸诱导的失活构象变化。
A deactivating conformational change induced by reduced nicotinamide-adenine dinucleotide phosphate in a Neurospora glutamate dehydrogenase.
作者信息
Gore M G, Iwatsubo M
出版信息
Biochem J. 1975 Apr;147(1):181-4. doi: 10.1042/bj1470181.
Abstract
Stopped-flow fluorescence techniques have been used to observe the formation of the binary comples of E-NADPH. At pH 7.5 there is a protein conformational change after the formation of the binary complex. This conformational change can be detected by a decrease in the fluorescence intensity of the complex at 350 nm and by an increase in its fluorescence intensity at 450 nm.
摘要
停流荧光技术已被用于观察E-NADPH二元复合物的形成。在pH 7.5时，二元复合物形成后会发生蛋白质构象变化。这种构象变化可以通过复合物在350nm处荧光强度的降低以及在450nm处荧光强度的增加来检测。
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本文引用的文献
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Biochem J. 1972 Jul;128(4):933-40. doi: 10.1042/bj1280933.
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Allosteric effects in nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase from Neurospora.来自脉孢菌的烟酰胺腺嘌呤二核苷酸磷酸特异性谷氨酸脱氢酶中的变构效应。
J Biol Chem. 1967 May 10;242(9):2134-8.
3
Slow conformational changes of a Neurospora glutamate dehydrogenase studied by protein fluorescence.通过蛋白质荧光研究的粗糙脉孢菌谷氨酸脱氢酶的缓慢构象变化。
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