氧化型谷胱甘肽对红细胞某些酶的影响及其与红细胞酶活性和电泳迁移率的关系。
Effect of oxidized glutathione on some enzymes of erythrocytes and its relation to erythrocytic enzyme activity and electrophoretic mobility.
作者信息
Walter H, Caccam J F
出版信息
Biochem J. 1966 Jul;100(1):274-7. doi: 10.1042/bj1000274.
Abstract
- Oxidized glutathione reacts or interacts with some erythrocytic enzymes (glucose 6-phosphate dehydrogenase, EC 1.1.1.49, aspartate aminotransferase, EC 2.6.1.10) but not with some others (lactate dehydrogenase, EC 1.1.1.27). 2. GSSG does not diminish the activity of any of these enzymes and is therefore not responsible for the decreased enzyme activities associated with older erythrocytes. 3. It may be that the reaction of aspartate aminotransferase with GSSG is the cause for the more rapid anodic electrophoretic mobility of this enzyme derived from human erythrocytes when compared with the mobility of the same enzyme from other human tissues. 4. A reinterpretation of some related, previously published, data with regard to the electrophoretic mobility of the above-mentioned enzymes from young and old erythrocytes is presented.
摘要
- 氧化型谷胱甘肽与一些红细胞酶（葡萄糖6-磷酸脱氢酶，EC 1.1.1.49，天冬氨酸氨基转移酶，EC 2.6.1.10）发生反应或相互作用，但不与其他一些酶（乳酸脱氢酶，EC 1.1.1.27）发生反应或相互作用。2. 氧化型谷胱甘肽不会降低这些酶中任何一种的活性，因此它与衰老红细胞中酶活性降低无关。3. 与来自其他人体组织的同一种酶的迁移率相比，天冬氨酸氨基转移酶与氧化型谷胱甘肽的反应可能是源自人体红细胞的该酶阳极电泳迁移率更快的原因。4. 对先前发表的有关上述酶在年轻和衰老红细胞中电泳迁移率的一些相关数据进行了重新解读。
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Studies on the heterogeneity of hemoglobin. V. Binding of hemoglobin with oxidized glutathione.血红蛋白异质性研究。V. 血红蛋白与氧化型谷胱甘肽的结合
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