Characterization of reverse transcriptase from feline immunodeficiency virus

Thomas W. North, Richard C. Cronn, Kathryn Martin Remington, Rolf T. Tandberg, Ralph C. Judd

Research output: Contribution to journalArticle

49 Scopus citations

Abstract

Reverse transcriptase has been purified from feline immunodeficiency virus (FIV) by DEAE-cellulose and phosphocellulose chromatography. The purified enzyme consists of a single protein with a Mr of 67,000. When proteolysis is not minimized during purification, a fragment of Mr 54,000 is also observed. This is similar to the reverse transcriptase from human immunodeficiency virus type 1 (HIV), which consists of a polypeptide of Mr 66,000; when proteolysis is not minimized during purification, a fragment of Mr 51,000 is also observed. In direct comparisons, the FIV reverse transcriptase is very similar to the HIV reverse transcriptase in template specificity and requirements for Mg2+. In contrast to these similarities, the FIV and HIV reverse transcriptases are substantially different in primary sequence, as determined by peptide mapping.

Original languageEnglish (US)
Pages (from-to)5121-5128
Number of pages8
JournalJournal of Biological Chemistry
Volume265
Issue number9
StatePublished - 1990
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Characterization of reverse transcriptase from feline immunodeficiency virus'. Together they form a unique fingerprint.

  • Cite this

    North, T. W., Cronn, R. C., Remington, K. M., Tandberg, R. T., & Judd, R. C. (1990). Characterization of reverse transcriptase from feline immunodeficiency virus. Journal of Biological Chemistry, 265(9), 5121-5128.