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- W1624440538 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." @default.
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- W1624440538 date "1990-03-01" @default.
- W1624440538 modified "2023-09-27" @default.
- W1624440538 title "Characterization of reverse transcriptase from feline immunodeficiency virus." @default.
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- W1624440538 doi "https://doi.org/10.1016/s0021-9258(19)34093-1" @default.
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