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[大鼠肝脏中的多核苷酸磷酸化酶:生长激素对其活性的分离与调节]

[Polynucleotide phosphorylase from rat liver: isolation and regulation of its activity by growth hormone].

作者信息

Andrianova L E, Khoroshutina E B, Fedotov V P, Votrin I I

出版信息

Biokhimiia. 1982 May;47(5):857-63.

PMID:7093386
Abstract

Using ion-filtration chromatography on DEAE-Sephadex A-25, a homogeneous polynucleotide phosphorylase having specific activity of 350--360 u./mg and containing no admixtures of nucleases or phosphatases was obtained. Injection of 32P phosphate to hypophysectomized animals was accompanied by the label incorporation into the enzyme molecule. The data obtained indirectly indicate that the enzyme is activated by phosphorylation and is inactivated by dephosphorylation, both processes being mediated by some factor found in liver cytosol of intact animals.

摘要

使用DEAE-葡聚糖A-25进行离子过滤色谱法,得到了一种比活性为350 - 360单位/毫克的均一的多核苷酸磷酸化酶,且该酶不含核酸酶或磷酸酶的杂质。向垂体切除的动物注射32P磷酸盐时,会伴随标记物掺入酶分子。所获得的数据间接表明,该酶通过磷酸化被激活,通过去磷酸化被失活,这两个过程均由完整动物肝细胞溶胶中发现的某种因子介导。

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Biokhimiia. 1982 May;47(5):857-63.
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