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柳氮磺胺吡啶的组织和细菌裂解

Tissue and bacterial splitting of sulphasalazine.

作者信息

Azad Khan A K, Guthrie G, Johnston H H, Truelove S C, Williamson D H

出版信息

Clin Sci (Lond). 1983 Mar;64(3):349-54. doi: 10.1042/cs0640349.

Abstract
  1. The cleavage of sulphasalazine at the azo bond by bacterial suspensions and tissue homogenates has been studied in vitro. 2. For maximum activity the azo reductase system requires anaerobic conditions and the presence of cofactors, namely NADPH and FAD. In this respect, sulphasalazine resembles other azo dyes. 3. Under optimum conditions all the species of bacteria tested were capable of splitting sulphasalazine and there were no major differences in the degree of activity shown by different species. The enzyme system is located within the bacterial cell and does not leak out of it. 4. All the tissues tested, both human and rat, showed azo reductase activity. The liver showed a much higher activity than the other tissues.
摘要
  1. 已在体外研究了细菌悬液和组织匀浆对柳氮磺胺吡啶偶氮键的裂解作用。2. 为达到最大活性,偶氮还原酶系统需要厌氧条件以及辅因子的存在,即还原型辅酶Ⅱ(NADPH)和黄素腺嘌呤二核苷酸(FAD)。在这方面,柳氮磺胺吡啶类似于其他偶氮染料。3. 在最佳条件下,所有测试的细菌种类都能够裂解柳氮磺胺吡啶,不同种类细菌所表现出的活性程度没有显著差异。酶系统位于细菌细胞内,不会从细胞中泄漏出来。4. 所有测试的组织,包括人类和大鼠的组织,都显示出偶氮还原酶活性。肝脏的活性比其他组织高得多。

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