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 language | English (US) |
|---|---|
| Pages (from-to) | 5121-5128 |
| Number of pages | 8 |
| Journal | Journal of Biological Chemistry |
| Volume | 265 |
| Issue number | 9 |
| State | Published - 1990 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
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 journal › Article
}
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.
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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 -