pubmed-article:8415662 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8415662 | lifeskim:mentions | umls-concept:C0013935 | lld:lifeskim |
pubmed-article:8415662 | lifeskim:mentions | umls-concept:C0012890 | lld:lifeskim |
pubmed-article:8415662 | lifeskim:mentions | umls-concept:C0013139 | lld:lifeskim |
pubmed-article:8415662 | pubmed:issue | 19 | lld:pubmed |
pubmed-article:8415662 | pubmed:dateCreated | 1993-11-10 | lld:pubmed |
pubmed-article:8415662 | pubmed:abstractText | We have purified a DNA polymerase activity from 0- to 2-hr embryos of Drosophila melanogaster to near homogeneity. The purified enzyme consists of a single 120-kDa polypeptide, which contains polymerase and 3'-->5' exonuclease activities. Exonuclease activity is inhibited by deoxynucleoside triphosphates, suggesting that the polymerase and exonuclease activities are coupled. The polymerase is more active with poly(dA-dT) than with activated DNA or poly(dA)/oligo(dT) as template. It shows a low degree of processivity with poly(dA)/oligo(dT). The polymerase is sensitive to aphidicolin and carbonyldiphosphonate but resistant to N2-[p-(n-butyl)phenyl]-2-deoxyguanosine triphosphate, 2-[p-(n-butyl)anilino]-2-deoxyadenosine triphosphate, and dideoxythymidine triphosphate. The 120-kDa polypeptide can be distinguished from the large subunit of Drosophila DNA polymerase alpha on the basis of the peptides generated by partial cleavage with N-chlorosuccinimide and by its failure to react with a monoclonal antibody directed against the large subunit of DNA polymerase alpha. The DNA polymerase is inhibited by 200 mM NaCl and is unable to use poly(rA)/oligo(dT) as a template, thus differentiating it from DNA polymerase gamma. On the basis of these properties, we propose that the DNA polymerase that we have purified from 0- to 2-hr Drosophila melanogaster embryos is DNA polymerase delta. | lld:pubmed |
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pubmed-article:8415662 | pubmed:language | eng | lld:pubmed |
pubmed-article:8415662 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8415662 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8415662 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8415662 | pubmed:month | Oct | lld:pubmed |
pubmed-article:8415662 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:8415662 | pubmed:author | pubmed-author:LehmanI RIR | lld:pubmed |
pubmed-article:8415662 | pubmed:author | pubmed-author:ChiangC SCS | lld:pubmed |
pubmed-article:8415662 | pubmed:author | pubmed-author:MitsisP GPG | lld:pubmed |
pubmed-article:8415662 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8415662 | pubmed:day | 1 | lld:pubmed |
pubmed-article:8415662 | pubmed:volume | 90 | lld:pubmed |
pubmed-article:8415662 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8415662 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8415662 | pubmed:pagination | 9105-9 | lld:pubmed |
pubmed-article:8415662 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:8415662 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8415662 | pubmed:articleTitle | DNA polymerase delta from embryos of Drosophila melanogaster. | lld:pubmed |
pubmed-article:8415662 | pubmed:affiliation | Department of Biochemistry, Beckman Center, Stanford University, CA 94305. | lld:pubmed |
pubmed-article:8415662 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8415662 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
entrez-gene:39746 | entrezgene:pubmed | pubmed-article:8415662 | lld:entrezgene |
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