| Literature DB >> 2432165 |
E M Wondrak, J Löwer, R Kurth.
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 X (dG)12-18 as template-primer. Kinetic data (Michaelis constant, Hill coefficient) were calculated for several substrates.Entities:
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Year: 1986 PMID: 2432165 DOI: 10.1099/0022-1317-67-12-2791
Source DB: PubMed Journal: J Gen Virol ISSN: 0022-1317 Impact factor: 3.891