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狒狒内源性病毒DNA聚合酶的纯化与特性分析

Purification and characterization of baboon endogenous virus DNA polymerase.

作者信息

Sarin P S, Friedman B, Gallo R C

出版信息

Biochim Biophys Acta. 1977 Nov 16;479(2):198-206. doi: 10.1016/0005-2787(77)90140-x.

DOI:10.1016/0005-2787(77)90140-x
PMID:200268
Abstract

An RNA-directed DNA polymerase was purified from baboon endogenous type-C virus by successive column chromatography on DEAE cellulose, phosphocellulose and hydroxyapatite. The purified DNA polymerase has a molecular weight of 68 000, a pH optimum of 8.0, a Mn2+ optimum of 1 mM, and a KCl optimum of 40 mM. The purified enzyme transcribes heteropolymeric regions of viral 60--70 S RNA isolated from different type-C viruses. The purified enzyme is immunologically related to a similarly purified polymerase from the cat endogenous type-C virus RD114.

摘要

通过在二乙氨基乙基纤维素、磷酸纤维素和羟基磷灰石上连续柱层析，从狒狒内源性C型病毒中纯化出一种RNA指导的DNA聚合酶。纯化的DNA聚合酶分子量为68000，最适pH为8.0，最适锰离子浓度为1 mM，最适氯化钾浓度为40 mM。该纯化酶能转录从不同C型病毒分离的病毒60 - 70 S RNA的异聚区域。纯化的酶与从猫内源性C型病毒RD114中类似纯化的聚合酶存在免疫相关性。

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