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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1996-8-15
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pubmed:abstractText |
We investigated nuclease activities associated with the catalytic subunit of herpes simplex virus type 1 DNA polymerase. We confirm that a 3'-5' exonuclease copurifies with this enzyme. Previous reports suggested that a 5' DNase was intrinsic to the polymerase. Our preparation lacks such activity.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0022-538X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
70
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4816-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8676514-Animals,
pubmed-meshheading:8676514-Cell Line,
pubmed-meshheading:8676514-DNA-Directed DNA Polymerase,
pubmed-meshheading:8676514-Exodeoxyribonuclease V,
pubmed-meshheading:8676514-Exodeoxyribonucleases,
pubmed-meshheading:8676514-Herpesvirus 1, Human,
pubmed-meshheading:8676514-Humans,
pubmed-meshheading:8676514-Mutation,
pubmed-meshheading:8676514-Spodoptera,
pubmed-meshheading:8676514-Substrate Specificity,
pubmed-meshheading:8676514-Viral Proteins
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pubmed:year |
1996
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pubmed:articleTitle |
Evidence that the nuclease activities associated with the herpes simplex type 1 DNA polymerase are due to the 3'-5' exonuclease.
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pubmed:affiliation |
Department of Molecular and Cellular Biology, University of Arizona, Tucson, Arizona 85721, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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