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. 1978 Nov;28(2):427–433. doi: 10.1128/jvi.28.2.427-433.1978

Detergent-inhibited, heat-labile nucleoside triphosphatase in cores of avian myeloblastosis virus.

K F Jensen
PMCID: PMC354291  PMID: 214571

Abstract

Endogenous DNA synthesis was studied in isolated core particles of avian myeloblastosis virus. It was found that cores contained an enzymatic activity which rapidly converted the added nucleoside triphosphates to diphosphates (but not further) at 0 degrees C, thus inhibiting DNA synthesis. This triphosphatase probably originates from the viral membranes. In the cores the enzyme is completely inactivated by low concentrations (0.02%) of Nonident P-40. Also, the enzyme is very thermolabile and denatures rapidly at 38 degrees C.

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Selected References

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