Characterization of reverse transcriptase from feline immunodeficiency virus.
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.
North
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Division of Biological Sciences, University of Montana, Missoula 59812.
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Remington
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Tandberg
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Judd
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D000818:Animals; D002371:Cat Diseases / Q000382:microbiology*; D002415:Cats; D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D007153:Immunologic Deficiency Syndromes / Q000382:microbiology / Q000662:veterinary*; D007700:Kinetics; D008970:Molecular Weight; D010447:Peptide Hydrolases; D010449:Peptide Mapping; D011131:Polyribonucleotides; D012194:RNA-Directed DNA Polymerase / Q000302:isolation & purification / Q000378:metabolism*; D012190:Retroviridae / Q000201:enzymology*; D013698:Templates, Genetic
D011131:Polyribonucleotides; D012194:RNA-Directed DNA Polymerase; D010447:Peptide Hydrolases