HIV-1 Reverse Transcriptase Purified from a Recombinant Strain of Escherichia coli

P. K. Clark, A. L. Ferris, D. A. Miller, A. Hizi, K. W. Kim, S. M. Deringer Boyer, M. L. Mellini, A. D. Clark, G. F. Arnold, W. B. Lebherz, E. Arnold, G. M. Muschik, S. H. Hughes

Research output: Contribution to journalArticlepeer-review

Abstract

A better understanding of the structure and biochemical properties of the replicative machinery of human immunodeficiency virus type 1 (HIV-1) may be useful in the screening and design of drugs that could be used to treat AIDS. We have previously described a recombinant strain of Escherichia coli that produces HIV-1 reverse transcriptase (RT). Fermentation conditions for the large-scale growth of the bacterial strain and a protocol for the purification of an enzymatically active 66-Kd form of the RT have been developed. The purified RT has all of the appropriate enzymatic functions and properties. The recombinant protein can be substituted for the viral enzyme in structural and biochemical studies and used in screens for drugs that could inhibit HIV replication.

Original languageEnglish
Pages (from-to)753-764
Number of pages12
JournalAIDS Research and Human Retroviruses
Volume6
Issue number6
DOIs
StatePublished - Jun 1990

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