Purification of virus-like particles of recombinant human papillomavirus type 11 major capsid protein L1 from Saccharomyces cerevisiae

被引：95

作者：

Cook, JC

Joyce, JG

George, HA

Schultz, LD

Hurni, WM

Jansen, KU

Hepler, RW

Ip, C

Lowe, RS

Keller, PM

Lehman, ED

机构：

[1] Department of Virus and Cell Biology, Merck Research Laboratories, West Point

[2] Dept. Vacc. BioProcess Research D., Merck Research Laboratories, West Point

来源：

PROTEIN EXPRESSION AND PURIFICATION | 1999年 / 17卷 / 03期

关键词：

D O I：

10.1006/prep.1999.1155

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Recombinant major capsid protein, L1 (M-r = 55,000), of human papillomavirus type 11 was expressed intracellularly at high levels in a galactose-inducible Saccharomyces cerevisiae expression system by an HPV6/11 hybrid gene. The capsid protein self-assembled into virus-like particles (VLPs) and accounted for 15% of the total soluble protein. A purification process was developed that consisted of two main steps: microfiltration and cation-exchange chromatography. The purified VLPs were 98% homogeneous, and the overall purification yield was 10%. The final product was characterized by several analytical methods and was highly immunogenic in mice. (C) 1999 Academic Press.

引用

页码：477 / 484

页数：8

共 30 条

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