An efficient procedure for the expression and purification of HIV-1 protease from inclusion bodies
Authors:
- 1 December 2015
- journal article
- Published by Elsevier in Protein Expression and Purification
- Vol. 116, 59-65
Abstract
No abstract availableKeywords
Funding Information
- Ministry of Science and Technology (ĐT- PTNTĐ.2012-G/02)
This publication has 12 references indexed in Scilit:
- Optimizing HIV-1 protease production in Escherichia coli as fusion proteinMicrobial Cell Factories, 2011
- Structural Analysis of Human Immunodeficiency Virus Type 1 CRF01_AE Protease in Complex with the Substrate p1-p6Journal of Virology, 2008
- Development of HIV-1 protease expression methods using the T7 phage promoter systemApplied Microbiology and Biotechnology, 1997
- HIV-I proteaseApplied Biochemistry and Biotechnology, 1996
- Kinetics and mechanism of autoprocessing of human immunodeficiency virus type 1 protease from an analog of the Gag-Pol polyprotein.Proceedings of the National Academy of Sciences, 1994
- Cloning, expression and purification of a recombinant poly‐histidine‐linked HIV‐1 proteaseFEBS Letters, 1993
- Large scale purification and refolding of HIV-1 protease fromEscherichia coli inclusion bodiesThe Protein Journal, 1993
- High-level production of active HIV-1 protease in Escherichia coliGene, 1992
- High-level synthesis of recombinant HIV-1 protease and the recovery of active enzyme from inclusion bodiesGene, 1990
- Chemical synthesis and enzymatic activity of a 99-residue peptide with a sequence proposed for the human immunodeficiency virus protease.Proceedings of the National Academy of Sciences, 1988