Ribonuclease H activity present in purified DNA polymerase from avian myeloblastosis virus

The presence of ribonuclease H activity in the purified complex of DNA polymerase from avian myeloblastosis virus is described. Evidence includes co-chromatography of the two activities during all purification steps; the presence of ribonuclease H activity in the purified two-polypeptide complex of...

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Veröffentlicht in:	Biochemical and biophysical research communications 1973-03, Vol.51 (1), p.232-240
Hauptverfasser:	Watson, K.F., Mölling, K., Bauer, H.
Format:	Artikel
Sprache:	eng
Schlagworte:	Antibodies, Viral Avian Leukosis Virus - enzymology Avian Leukosis Virus - isolation & purification DNA Nucleotidyltransferases - isolation & purification DNA Nucleotidyltransferases - metabolism DNA-Directed RNA Polymerases - metabolism Escherichia coli - enzymology Nucleic Acid Hybridization Ribonucleases - metabolism Time Factors Tritium Viral Proteins - analysis
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Zusammenfassung:	The presence of ribonuclease H activity in the purified complex of DNA polymerase from avian myeloblastosis virus is described. Evidence includes co-chromatography of the two activities during all purification steps; the presence of ribonuclease H activity in the purified two-polypeptide complex of DNA polymerase; ion requirements for optimal activity of purified ribonuclease H are identical to those for the purified DNA polymerase; and monospecific antiserum against purified DNA polymerase neutralizes the ribonuclease H activity.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/0006-291X(73)90533-0