Functional Purification and Enzymic Characterization of the RNA-dependent DNA Polymerase of Human Immunodeficiency Virus
- 1 December 1986
- journal article
- research article
- Published by Microbiology Society in Journal of General Virology
- Vol. 67 (12) , 2791-2797
- https://doi.org/10.1099/0022-1317-67-12-2791
Abstract
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 .cntdot. (dG)12-18 as template-primer. Kinetic data (Michaelis constant, Hill coefficient) were calculated for several substrates.This publication has 13 references indexed in Scilit:
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