PMID: 6160261Aug 1, 1980Paper

Simple affinity procedure for the purification of mammalian viral reverse transcriptases

Journal of Virology
M G SarngadharanR C Gallo

Abstract

Polyguanylic acid was found to be a potent inhibitor of RNase H associated with mammalian viral reverse transcriptase, indicating a strong interaction between polyguanylic acid and the reverse transcriptase protein. Based on this observation, we have developed three simple procedures for the purification of mammalian viral reverse transcriptases. In the first procedure, a nucleic acid-free extract of Rauscher murine leukemia virus was applied to a column of phosphocellulose and the reverse transcriptase was eluted by a low concentration (50 microM) of polyguanylic acid. Polyadenylic acid and polyuridylic acid could not replace polyguanylic acid for the elution. In the second procedure, a polyuridylic acid-Sepharose column was substituted for phosphocellulose, and the elution was again achieved by polyguanylic acid. In the third affinity procedure, the reverse transcriptase in a nucleic acid-free viral extract was incubated in the cold with 50 microM polyguanylic acid and the complex was adsorbed onto a DEAE-cellulose column. After washing to remove uncomplexed and weakly complexed proteins, the reverse transcriptase was eluted in a concentrated form at 0.3 M NaCl with a recovery of greater than 70%. by polyacrylamide gel analys...Continue Reading

References

May 17, 1974·Biochimica Et Biophysica Acta·B J LewisR C Gallo
Sep 24, 1971·Biochimica Et Biophysica Acta·D L KacianS Spiegelman

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Citations

Nov 15, 1985·International Journal of Cancer. Journal International Du Cancer·P C Jacquemin, P Strijckmans
Dec 1, 1981·Analytical Biochemistry·A J ParkinsonH G Muchmore

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