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大鼠肝脏制剂催化芳烷基硫酸酯与谷胱甘肽的反应。

The reaction of aralkyl sulphate esters with glutathione catalysed by rat liver preparations.

作者信息

Gillham B

出版信息

Biochem J. 1971 Feb;121(4):667-72. doi: 10.1042/bj1210667.

Abstract
  1. Rat liver supernatant preparations catalyse the reactions of some aralkyl sulphate esters with GSH to yield S-aralkylglutathione derivatives. 2. A glutathione S-transferase that catalyses these reactions has been purified 16-fold. 3. The purified enzyme preparation catalyses the release of sulphate ions from benzyl sulphate, 1-menaphthyl (naphth-1-ylmethyl) sulphate and phenanthr-9-ylmethyl sulphate only in the presence of GSH. It does not cause the release of sulphate ions from prop-1-yl sulphate, l-serine O-sulphate, phenyl sulphate or oestrone 3-sulphate even when GSH is added. 4. The stability and specificity of the enzyme and its response to inhibitors and to changes of pH were studied. 5. The activity of the preparation was compared with the activities of glutathione S-transferases described previously.
摘要
  1. 大鼠肝脏上清液制剂催化某些芳烷基硫酸酯与谷胱甘肽(GSH)反应,生成S-芳烷基谷胱甘肽衍生物。2. 一种催化这些反应的谷胱甘肽S-转移酶已被纯化了16倍。3. 纯化的酶制剂仅在存在GSH的情况下,催化从硫酸苄酯、1-甲萘基(萘-1-基甲基)硫酸酯和菲-9-基甲基硫酸酯中释放硫酸根离子。即使添加了GSH,它也不会导致从丙-1-基硫酸酯、L-丝氨酸O-硫酸酯、硫酸苯酯或雌酮3-硫酸酯中释放硫酸根离子。4. 研究了该酶的稳定性、特异性及其对抑制剂和pH变化的反应。5. 将该制剂的活性与先前描述的谷胱甘肽S-转移酶的活性进行了比较。

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Glutathione S-aralkyltransferase.谷胱甘肽S-芳烷基转移酶
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