Page M G, Burton K
Biochem J. 1978 Sep 15;174(3):717-25. doi: 10.1042/bj1740717.
During the preparation of spheroplasts, adenine phosphoribosyltransferase (EC 2.4.2.7) and hypoxanthine phosphoribosyltransferase (EC 2.4.2.8) were released in parallel with cytidine deaminase (EC 3.5.4.5) and uridine phosphorylase (EC 2.4.2.3), which, on other evidence, are considered to be located intracellularly. The two phosphoribosyltransferases and uridine phosphorylase were not significantly associated with purified membrane fractions as was purine nucleoside phosphorylase (EC 2.4.2.1). The effects of the poorly permeable enzyme-inactivating reagents, 4-diazoniumbenzenesulphonate, 7-diazonium-1,3-naphthalene-disulphonate and 2,4,6-trinitrobenzenesulphonate, on Escherichia coli indicate that all the above-mentioned enzymes and also the xanthine-guanine phosphoribosyltransferase [Miller, Ramsey, Krenitsky & Elion (1972) Biochemistry 11, 4723--4731] are located intracellularly.
在制备原生质球的过程中,腺嘌呤磷酸核糖转移酶(EC 2.4.2.7)和次黄嘌呤磷酸核糖转移酶(EC 2.4.2.8)与胞苷脱氨酶(EC 3.5.4.5)和尿苷磷酸化酶(EC 2.4.2.3)同时释放,根据其他证据,这些酶被认为位于细胞内。这两种磷酸核糖转移酶和尿苷磷酸化酶与纯化的膜组分没有明显关联,而嘌呤核苷磷酸化酶(EC 2.4.2.1)则不然。渗透性差的酶失活试剂4-重氮苯磺酸盐、7-重氮-1,3-萘二磺酸盐和2,4,6-三硝基苯磺酸盐对大肠杆菌的作用表明,上述所有酶以及黄嘌呤-鸟嘌呤磷酸核糖转移酶[米勒、拉姆齐、克雷尼茨基和埃利昂(1972年)《生物化学》11, 4723 - 4731]都位于细胞内。