1887

Abstract

Summary

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 Mg for optimal activity except with (C)·(dG) as template-primer. Kinetic data (Michaelis constant, Hill coefficient) were calculated for several substrates.

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/content/journal/jgv/10.1099/0022-1317-67-12-2791
1986-12-01
2019-11-18
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http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-67-12-2791
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