在小鼠谷胱甘肽转移酶催化的反应中形成的4-硝基喹啉1-氧化物的谷胱甘肽共轭物的鉴定。
Identification of the glutathione conjugate of 4-nitroquinoline 1-oxide formed in the reaction catalyzed by murine glutathione transferases.
作者信息
Stanley J S, Lay J O, Miller D W, DeLuca D C
机构信息
Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock 72205.
出版信息
Carcinogenesis. 1989 Mar;10(3):587-91. doi: 10.1093/carcin/10.3.587.
The product of the enzyme-catalyzed conjugation of glutathione and 4-nitroquinoline 1-oxide was isolated and its structure determined by MS and NMR. The results indicate that the cysteine sulfur of glutathione replaces the nitro group of 4-nitroquinoline 1-oxide in the reaction with the formation of 4-(glutathion-S-yl)-quinoline 1-oxide. No evidence was found for the binding of glutathione to any other position of 4-nitroquinoline 1-oxide or through any group other than the cysteine sulfur.
分离出了谷胱甘肽与4-硝基喹啉1-氧化物经酶催化共轭反应的产物，并通过质谱和核磁共振确定了其结构。结果表明，在反应中谷胱甘肽的半胱氨酸硫取代了4-硝基喹啉1-氧化物的硝基，形成了4-（谷胱甘肽-S-基）-喹啉1-氧化物。未发现谷胱甘肽与4-硝基喹啉1-氧化物的任何其他位置结合或通过半胱氨酸硫以外的任何基团结合的证据。
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