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衰老人晶状体中一部分谷胱甘肽还原酶的热稳定性改变。

Altered heat-lability of a fraction of glutathione reductase in aging human lens.

作者信息

Harding J J

出版信息

Biochem J. 1973 Aug;134(4):995-1000. doi: 10.1042/bj1340995.

Abstract

An unusually heat-labile fraction of glutathione reductase appears in human lens at about an age of 32 years. No such change was found in glucose 6-phosphate dehydrogenase nor in 3-phosphoglycerate kinase. The change is an intrinsic property of glutathione reductase. A greater proportion of the altered glutathione reductase was found in the core, the older part, of the lens. No evidence of a second band of activity was obtained after electrophoresis. Possible interpretations of the results, including errors of protein synthesis, production of a new isoenzyme and post-synthetic changes, are discussed.

摘要

一种异常不耐热的谷胱甘肽还原酶组分大约在32岁时出现在人晶状体中。在葡萄糖6 - 磷酸脱氢酶和3 - 磷酸甘油酸激酶中未发现此类变化。这种变化是谷胱甘肽还原酶的一种内在特性。在晶状体较老的核心部分发现了更大比例的改变后的谷胱甘肽还原酶。电泳后未获得第二条活性带的证据。讨论了对结果的可能解释,包括蛋白质合成错误、新同工酶的产生和合成后变化。

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本文引用的文献

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Altered enzymes in ageing human fibroblasts.衰老人类成纤维细胞中的酶变化
Nature. 1972 Jul 7;238(5358):26-30. doi: 10.1038/238026a0.
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Protein synthesis in the core of calf lens.小牛晶状体核心中的蛋白质合成。
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