首页 | 本学科首页   官方微博 | 高级检索  
     


Large scale expression and purification of recombinant HIV-1 proteinase from Escherichia coli.
Authors:O M Singh  D S Baines  R M Hall  N M Gray  M P Weir
Affiliation:Department of Genetics, Glaxo Group Research Ltd., Greenford, Middlesex, U.K.
Abstract:The availability of target proteins in sufficient quantity is a limiting factor in crystallographic studies and therefore in rational drug design. Even after optimisation, expression of recombinant proteins may be low and the only way to produce enough protein is by large scale cell growth/purification. HIV-1 proteinase in Escherichia coli, which due to its toxicity is expressed as a soluble protein only at around 0.1% of total protein, is a paradigm for this. In this paper a detailed process for large scale expression and purification of HIV-1 proteinase which delivers material of suitable quantity (30 mg from 500 g of wet weight of cells) and quality for crystallographic studies is described.
Keywords:
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号