Article
Isolation of mutants of human immunodeficiency virus protease based on the toxicity of the enzyme in Escherichia coli.
Proceedings of the National Academy of Sciences of the United States of America - 1 Jul 1990
Baum E Z, Bebernitz G A, Gluzman Y
Abstract excerpt
The protease encoded by the pol gene of human immunodeficiency virus was expressed in Escherichia coli and found to be toxic to strain BL21(DE3). This toxicity provided a convenient selection for isolating mutants of the protease that are nontoxic and enzymatically inactive. This strong correlation between functional protease and toxicity resulted in rapid identification of several protease mutations, including...
Topics
- Base Sequence
- Cloning, Molecular
- Codon
- Escherichia coli
- Gene Products, pol
- HIV
- Kinetics
- Molecular Sequence Data
- Mutation
- Oligonucleotide Probes
- Peptide Hydrolases