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J Gen Virol 67 (1986), 2791-2797; DOI 10.1099/0022-1317-67-12-2791
© 1986 Society for General Microbiology
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Functional Purification and Enzymic Characterization of the RNA-dependent DNA Polymerase of Human Immunodeficiency Virus

E. M. Wondrak, J. Löwer and R. Kurth

Paul-Ehrlich-Institut, Paul-Ehrlich-Strasse 42-44, D-6000 Frankfurt am Main 70, F.R.G.

The RNA-dependent DNA polymerase (RDDP) of human immunodeficiency virus (HIV) was purified from sucrose density gradient-banded virus by four successive procedures: anion exchange chromatography, cation exchange chromatography, affinity chromatography on oligo(dT)-cellulose and adsorption chromatography on hydroxyapatite. The enzyme preparation was free of cellular DNA-dependent DNA polymerase activity. The properties of HIV RDDP were determined with a variety of template-primers. Generally, the enzyme used Mg2+ for optimal activity except with (Cm)n·(dG)12–18 as template-primer. Kinetic data (Michaelis constant, Hill coefficient) were calculated for several substrates.

Keywords: HIV, reverse transcriptase, RNA-dependent DNA polymerase, AIDS

Received 6 May 1986; accepted 28 August 1986.


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