Affinity purification of HIV-1 and HIV-2 proteases from recombinant E. coli strains using pepstatin-agarose
- 1 August 1990
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 171 (1) , 60-66
- https://doi.org/10.1016/0006-291x(90)91356-w
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- High-level synthesis of recombinant HIV-1 protease and the recovery of active enzyme from inclusion bodiesGene, 1990
- Inhibition of HIV-1 protease in infected T-lymphocytes by synthetic peptide analoguesNature, 1990
- Purification, Assay and Kinetic Features of HIV-1 ProteinaseBiological Chemistry Hoppe-Seyler, 1990
- Crystallizable HIV-1 protease derived from expression of the viral pol gene in Escherichia coliBiochemical and Biophysical Research Communications, 1989
- Affinity purification of the HIV-1 proteaseBiochemical and Biophysical Research Communications, 1989
- Inhibition of the aspartic proteinase from HIV‐2FEBS Letters, 1989
- Effective blocking of HIV‐1 proteinase activity by characteristic inhibitors of aspartic proteinasesFEBS Letters, 1989
- Genetic locus, primary structure, and chemical synthesis of human immunodeficiency virys proteaseGene Analysis Techniques, 1988
- Complete purification of dog renal reninBiochemistry, 1979
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976