A Reappraisal of the γ-Glutamylcysteine Synthetase Activity in Haemolysates from Normal Erythrocytes by Two Different Methods
A Reappraisal of the γ-Glutamylcysteine Synthetase Activity in Haemolysates from Normal Erythrocytes by Two Different Methods
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通过两种不同的方法重新评估正常红细胞溶血产物中的γ-谷氨酰半胱氨酸合成酶活性
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发表时间：
1983
期刊：
影响因子：
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通讯作者：
J. White
中科院分区：
文献类型：
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作者：
A. N. Lestas;J. White
γ-谷氨酰半胱氨酸合成酶催化l-谷氨酸和l-半胱氨酸结合形成γ-谷氨酰半胱氨酸，并将ATP转化为ADP和无机磷酸盐（Pi）。在对正常红细胞血液溶解液中这种酶的估计中，发现Pi的释放量大于γ-谷氨酰半胱氨酸的合成量。此外，通过分析任何一种产品估计的活性都高于文献中报道的相应值。对这些差异的研究改进了检测方法，产生了血液中γ-谷氨酰半胱氨酸合成酶活性的两个基本不同的正常范围：一个来自释放的Pi，另一个来自酶促反应中合成的γ-谷氨酰半胱氨酸。
γ-Glutamylcysteine synthetase catalyses the combination of l-glutamate and l-cysteine to form γ-glutamylcysteine with a stoichiometric conversion of ATP to ADP and inorganic phosphate (Pi). During the estimation of this enzyme in haemolysates from normal erythrocytes it was found that the Pi released was more than the amount of γ-glutamylcysteine synthesised. Furthermore, the activity estimated by analysing either product was higher than the corresponding values reported in the literature. An investigation into these discrepancies resulted in improvements of the assay methods which produced two substantially different normal ranges for the γ-glutamylcysteine synthetase activity in haemolysates: one derived from the Pi released and the other from the γ-glutamylcysteine synthesised during the enzymatic reaction.