血红蛋白氧化后谷胱甘肽过氧化物酶的失活。
Inactivation of glutathione peroxidase following hemoglobin oxidation.
作者信息
Grelloni F, Gabbianelli R, Falcioni G
机构信息
Department of Molec., Cell. and Animal Biology, University of Camerino, Italy.
出版信息
Biochem Int. 1991 Dec;25(5):789-95.
PMID:1804099
Abstract
Inactivation of erythrocyte GSH-peroxidase correlates with the rate of hemoglobin oxidation. The presence of superoxide dismutase and catalase only marginally reduces the rate of inactivation of the enzyme indicating that the loss of activity is not due to oxygen radicals produced during oxidation of hemoglobin. The inactivation of glutathione peroxidase is due by-and-large to the formation of hemichromes.
摘要
红细胞谷胱甘肽过氧化物酶的失活与血红蛋白氧化速率相关。超氧化物歧化酶和过氧化氢酶的存在仅略微降低了该酶的失活速率，这表明活性丧失并非由于血红蛋白氧化过程中产生的氧自由基所致。谷胱甘肽过氧化物酶的失活在很大程度上是由于高铁血红素的形成。
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