氧化型谷胱甘肽对肝脏葡萄糖-6-磷酸脱氢酶活性影响的批判性评价。
A critical appraisal of the effect of oxidized glutathione on hepatic glucose 6-phosphate dehydrogenase activity.
作者信息
Levy H R, Christoff M
出版信息
Biochem J. 1983 Sep 15;214(3):959-65. doi: 10.1042/bj2140959.
Abstract
Experiments were undertaken to elucidate the mechanism of the reversal of NADPH inhibition of rat liver glucose 6-phosphate dehydrogenase by oxidized gluthathione alone and in combination with a putative cofactor described by Eggleston & Krebs [(1974) Biochem. J. 138, 425-435]. Evidence is presented that this reversal is largely an artifact, caused by the incorrect application of a control assay procedure and a spurious effect of Zn2+ (added in order to inhibit glutathione reductase) in crude enzyme solutions. When the proper assay procedure is used and glutathione reductase is inhibited with low concentrations of Hg2+, glutathione addition has no effect on NADPH inhibition of glucose 6-phosphate dehydrogenase. No evidence was found for the existence of a cofactor that mediates an effect of glutathione on glucose 6-phosphate dehydrogenase.
摘要
开展了实验以阐明单独的氧化型谷胱甘肽以及与埃格尔斯顿和克雷布斯所描述的一种假定辅助因子联合使用时，逆转NADPH对大鼠肝脏葡萄糖6 - 磷酸脱氢酶抑制作用的机制[（1974年）《生物化学杂志》138卷，425 - 435页]。有证据表明，这种逆转很大程度上是一种假象，是由于对照测定程序应用不当以及粗酶溶液中Zn2 +（为抑制谷胱甘肽还原酶而添加）的虚假效应所致。当使用正确的测定程序并用低浓度Hg2 +抑制谷胱甘肽还原酶时，添加谷胱甘肽对NADPH抑制葡萄糖6 - 磷酸脱氢酶没有影响。未发现存在介导谷胱甘肽对葡萄糖6 - 磷酸脱氢酶作用的辅助因子的证据。
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