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牛胰核糖核酸酶二硫键与谷胱甘肽的反应活性

The reactivity of the disulphide bonds of bovine pancreatic ribonuclease with glutathione.

作者信息

Davidson B E, Hird F J

出版信息

Biochem J. 1965 Sep;96(3):890-4. doi: 10.1042/bj0960890.

Abstract
  1. Bovine pancreatic ribonuclease is not reduced by GSH at near-physiological concentrations and pH. 2. Disruption of the structure of ribonuclease by proteolytic enzymes leads to products that can be reduced by GSH. 3. At higher temperatures the disulphide bonds of ribonuclease are completely reduced by GSH in a coupled system. The T(tr) is 51 degrees and this has been found to be lower than the T(tr) for the abnormal tyrosine residues under the same conditions.
摘要
  1. 在接近生理浓度和pH值的条件下,谷胱甘肽(GSH)不会使牛胰核糖核酸酶还原。2. 蛋白水解酶破坏核糖核酸酶的结构会产生可被谷胱甘肽还原的产物。3. 在较高温度下,核糖核酸酶的二硫键在偶联体系中会被谷胱甘肽完全还原。转变温度(T(tr))为51摄氏度,并且发现在相同条件下该温度低于异常酪氨酸残基的转变温度。

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本文引用的文献

1
Structure and function of ribonuclease.核糖核酸酶的结构与功能。
Adv Enzymol Relat Subj Biochem. 1962;24:161-261. doi: 10.1002/9780470124888.ch4.
2
Glutathione metabolism in animals.
Biochem Soc Symp. 1959;17:43-65.
3
Chemistry and biochemistry of glutathione.
Biochem Soc Symp. 1959;17:3-16.

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