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Article

Purification of HIV-1 wild-type protease and characterization of proteolytically inactive HIV-1 protease mutants by pepstatin A affinity chromatography.

FEBS letters - 25 Mar 1991

Wondrak E M, Louis J M, Mora P T, Oroszlan S

Abstract excerpt

Recombinant wild-type protease of human immunodeficiency virus, type 1 (HIV-1) expressed in E. coli was purified by pepstatin A affinity chromatography. An 88-fold purification was achieved giving a protease preparation with a specific enzymatic activity of approximately 3700 pmol/min/micrograms. Two proteolytically inactive HIV-1 mutant proteases (Arg-87----Lys; Asn-88----Glu) were found to bind to pepstatin A...

Topics

Amino Acid Sequence
Chromatography, Affinity
Endopeptidases
Escherichia coli
HIV Protease
HIV-1
Molecular Sequence Data
Mutation
Pepstatins
Recombinant Proteins

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Identifiers

PMID: 2013336
DOI: 10.1016/0014-5793(91)80328-z

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2013336-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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