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

47 Citations (Scopus)

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

Fingerprint

Feline Immunodeficiency Virus
RNA-Directed DNA Polymerase
Viruses
Proteolysis
HIV-1
Purification
DEAE-Cellulose Chromatography
DEAE-Cellulose
Peptides
Peptide Mapping
Chromatography
Enzymes
Human immunodeficiency virus 1 reverse transcriptase
Proteins

ASJC Scopus subject areas

  • Biochemistry

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.

Characterization of reverse transcriptase from feline immunodeficiency virus. / North, Thomas W.; Cronn, Richard C.; Remington, Kathryn Martin; Tandberg, Rolf T.; Judd, Ralph C.

In: Journal of Biological Chemistry, Vol. 265, No. 9, 1990, p. 5121-5128.

Research output: Contribution to journalArticle

North, TW, Cronn, RC, Remington, KM, Tandberg, RT & Judd, RC 1990, 'Characterization of reverse transcriptase from feline immunodeficiency virus', Journal of Biological Chemistry, vol. 265, no. 9, pp. 5121-5128.
North TW, Cronn RC, Remington KM, Tandberg RT, Judd RC. Characterization of reverse transcriptase from feline immunodeficiency virus. Journal of Biological Chemistry. 1990;265(9):5121-5128.
North, Thomas W. ; Cronn, Richard C. ; Remington, Kathryn Martin ; Tandberg, Rolf T. ; Judd, Ralph C. / Characterization of reverse transcriptase from feline immunodeficiency virus. In: Journal of Biological Chemistry. 1990 ; Vol. 265, No. 9. pp. 5121-5128.
@article{ae095ac133284408b7e6e61fc0b696ad,
title = "Characterization of reverse transcriptase from feline immunodeficiency virus",
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.",
author = "North, {Thomas W.} and Cronn, {Richard C.} and Remington, {Kathryn Martin} and Tandberg, {Rolf T.} and Judd, {Ralph C.}",
year = "1990",
language = "English (US)",
volume = "265",
pages = "5121--5128",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "9",

}

TY - JOUR

T1 - Characterization of reverse transcriptase from feline immunodeficiency virus

AU - North, Thomas W.

AU - Cronn, Richard C.

AU - Remington, Kathryn Martin

AU - Tandberg, Rolf T.

AU - Judd, Ralph C.

PY - 1990

Y1 - 1990

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0025248568&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025248568&partnerID=8YFLogxK

M3 - Article

C2 - 1690735

AN - SCOPUS:0025248568

VL - 265

SP - 5121

EP - 5128

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 9

ER -