PURIFICATION AND PROPERTIES OF THE HERPES-SIMPLEX VIRUS TYPE-1 UL8 PROTEIN

被引：24

作者：

PARRY, ME ^{[1
]}

STOW, ND ^{[1
]}

MARSDEN, HS ^{[1
]}

机构：

[1] INST VIROL,MRC,VIROL UNIT,CHURCH ST,GLASGOW G11 5JR,SCOTLAND

来源：

JOURNAL OF GENERAL VIROLOGY | 1993年 / 74卷

关键词：

D O I：

10.1099/0022-1317-74-4-607

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

A rapid and simple two-step scheme for the purification of herpes simplex virus type 1 UL8 protein from insect cells infected with a recombinant baculovirus has been developed. The scheme involves DEAE-Sepharose and phenyl-Sepharose chromatography and yields approximately 1.5 mg of protein from 2.4 x 10(8) infected cells. The protein remains intact during purification as judged by its reactivity with amino and carboxy termini-specific antisera. Gel filtration chromatography showed that the protein exists as a monomer in solution. No binding of the protein to ssDNA or dsDNA or to a DNA/RNA hybrid could be demonstrated using a gel mobility shift assay.

引用

页码：607 / 612

页数：6

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