Human hypoxanthine-guanine phosphoribosyltransferase.

Human hypoxanthine-guanine phosphoribosyltransferase.
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人次黄嘌呤鸟嘌呤磷酸核糖转移酶。

DOI:
10.1016/s0021-9258(19)45899-7
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发表时间:
1983
期刊:
The Journal of biological chemistry
影响因子:
--
通讯作者:
W. Kelley
W. Kelley
中科院分区:
--
文献类型:
--
作者:
J. Wilson;R. Kobayashi;I. Fox;W. Kelley

文献摘要

被引文献

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次黄嘌呤-鸟嘌呤磷酸核糖基转移酶(EC2.4.2.8)已从一名男性供体的人红细胞中纯化为均一。正常人类酶的斯托克斯半径为36A,分子量为68000,由两个分子量和净电荷相同的亚基组成,通过制备性等电聚焦可重复区分三种同工酶。这种电泳谱的异质性似乎是由一个或两个亚基的非遗传转录后改变引起的。
Hypoxanthine-guanine phosphoribosyltransferase (EC 2.4.2.8) has been purified to homogeneity from human erythrocytes obtained from one male donor. The normal human enzyme has a Stokes radius of 36 A with a molecular weight of 68,000 and is composed of two subunits which have identical molecular weight and net charge.Three isoenzymes were reproducibly distinguished by preparative isoelectric focusing. This electrophoretic heterogeneity appears to result from a nongenetic, post-transcriptional alteration of one or both subunits.