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Purification of HIV-1 Wild-Type Protease and Characterization of Proteolytically Inactive HIV-1 Protease Mutants by Pepstatin A Affinity Chromatography

Purification of HIV-1 Wild-Type Protease and Characterization of Proteolytically Inactive HIV-1 Protease Mutants by Pepstatin A Affinity Chromatography

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

FEBS Lett. 1991 Mar 25;280(2):347-50.

PMID: 2013336

Abstract:

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 agarose, and and they were purified as the wild-type protease. A third mutant protease Arg-87----Glu) was apparently unable to bind to pepstatin A under similar conditions. Binding to pepstatin A indicates the binding ability of the substrate binding site and the ability to form dimers. These features may be used to purify and to characterize other mutated HIV-1 proteases.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42411072	Pepstatin A−Agarose			Price

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