Presence of nucleoside triphosphate phosphohydrolase activity in purified virions of reovirus.

Journal of virology ·Vol. 6 ·No. 3 ·1970-09-00 ·Pages 295-302

Borsa J, Grover J, Chapman JD

Abstract

A nucleoside triphosphate phosphohydrolase activity has been discovered in reovirus virions. This activity converts nucleoside triphosphates to nucleoside diphosphates in vitro. Properties of this enzyme are presented, with evidence that this activity is an integral part of the virion core.

MeSH Terms

Animals Centrifugation, Density Gradient Chromatography, Thin Layer Hydrogen-Ion Concentration L Cells Lithium/pharmacology Magnesium Mice Ouabain/pharmacology Phosphates/pharmacology Phosphoric Monoester Hydrolases/metabolism Potassium/pharmacology RNA Nucleotidyltransferases/metabolism Reoviridae/enzymology Sodium/pharmacology Tritium Uridine/metabolism

Chemicals

Phosphates Tritium Ouabain Lithium Sodium RNA Nucleotidyltransferases Phosphoric Monoester Hydrolases Magnesium Potassium Uridine

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Borsa J

Grover J

Chapman J D

References (16)

16 references, click to expand

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Article Info

Journal

Journal of virology

Abbr.

J Virol

ISSN

0022-538X

DOI

10.1128/JVI.6.3.295-302.1970

Published

1970-09-00

Pages

295-302

Language

English

Region

United States

NLM ID

0113724

PMCID

PMC376122

Subset

External Links

PubMed source DOI: 10.1128/JVI.6.3.295-302.1970 PMC Full Text View journal details

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Presence of nucleoside triphosphate phosphohydrolase activity in purified virions of reovirus.

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