HIV-1 reverse transcriptase: polymerization properties of the p51 homodimer compared to the p66/p51 heterodimer.

doi:10.1021/bi00091a003

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Article

HIV-1 reverse transcriptase: polymerization properties of the p51 homodimer compared to the p66/p51 heterodimer.

Biochemistry - 12 Oct 1993

Bavand M R, Wagner R, Richmond T J

Abstract excerpt

The polymerase activity of the p51 homodimeric form of HIV reverse transcriptase was characterized by activity gel analysis, steady-state kinetic measurements, and processivity assays, and the activity was shown to be highly similar to that for the p66/p51 heterodimer. Recombinant 51- and 66-kDa...

Topics

Amino Acid Sequence
Base Sequence
DNA, Viral
Genes, pol
HIV Reverse Transcriptase
HIV-1
Kinetics
Macromolecular Substances
Molecular Sequence Data
Molecular Weight
Mutation
Oligodeoxyribonucleotides
RNA-Directed DNA Polymerase
Recombinant Proteins
Restriction Mapping

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Open in PubMed

Identifiers

PMID: 7691176
DOI: 10.1021/bi00091a003

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-7691176-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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