磷酸盐刺激大鼠腹侧前列腺对5'-甲硫腺苷的分解代谢
Phosphate-stimulated breakdown of 5'-methylthioadenosine by rat ventral prostate.
作者信息
Pegg A E, Williams-Ashman H G
出版信息
Biochem J. 1969 Nov;115(2):241-7. doi: 10.1042/bj1150241.
Abstract
A soluble enzyme preparation catalysing the release of adenine from 5'-methylthioadenosine was purified some 30-fold from extracts of the rat ventral prostate. This reaction was completely dependent on addition of inorganic phosphate ions to the assay medium. This absolute requirement for phosphate ions suggests a phosphorolytic cleavage mechanism. After acid treatment, the other product of the reaction appeared to be 5-methylthioribose. The actions of some other well-characterized enzymes of nucleoside metabolism of 5'-methylthioadenosine were also investigated; purified purine nucleoside phosphorylases from calf spleen and human erythrocytes did not attack 5'-methylthioadenosine. The role of 5'-methylthioadenosine in mammalian tissues is discussed.
摘要
一种可催化从5'-甲硫基腺苷释放腺嘌呤的可溶性酶制剂，从大鼠腹侧前列腺提取物中纯化了约30倍。该反应完全依赖于向测定培养基中添加无机磷酸根离子。对磷酸根离子的这种绝对需求表明存在磷酸解裂解机制。酸处理后，该反应的另一种产物似乎是5-甲硫基核糖。还研究了5'-甲硫基腺苷核苷代谢中其他一些特性明确的酶的作用；从小牛脾脏和人红细胞中纯化的嘌呤核苷磷酸化酶不作用于5'-甲硫基腺苷。讨论了5'-甲硫基腺苷在哺乳动物组织中的作用。
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