pubmed-article:351611 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:351611 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
pubmed-article:351611 | lifeskim:mentions | umls-concept:C0086972 | lld:lifeskim |
pubmed-article:351611 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:351611 | lifeskim:mentions | umls-concept:C1148807 | lld:lifeskim |
pubmed-article:351611 | lifeskim:mentions | umls-concept:C1704222 | lld:lifeskim |
pubmed-article:351611 | lifeskim:mentions | umls-concept:C0599123 | lld:lifeskim |
pubmed-article:351611 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:351611 | pubmed:dateCreated | 1978-9-1 | lld:pubmed |
pubmed-article:351611 | pubmed:abstractText | An in vitro complementation assay has been used for partial purification of uvrA+, uvrB+, and uvrC+ gene products from Escherichia coli. The uvrB+ and uvrC+ products cochromatograph on DEAE-cellulose and are completely resolved from the uvrA+ product, which has been further purified by phosphocellulose chromatography of the nonadsorbed protein fraction from the DEAE-cellulose. Neither the uvrB+/uvrC+ nor the uvrA+ product shows appreciable endonuclease activity on UV-irradiated DNA when tested separately. However, these factors complement each other to yield and ATP-dependent endonuclease activity specific for UV-irradiated DNA. Gel filtration experiments with the partially purified proteins indicate that the functional uvrA+ gene product has a molecular weight of 100,000. The uvrB+ gene product has an apparent molecular weight of 70,000, but it is presently unclear if this is the size of the uvrB+ product alone or the size of a complex of the uvrB+ and uvrC+ gene products. | lld:pubmed |
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pubmed-article:351611 | pubmed:language | eng | lld:pubmed |
pubmed-article:351611 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:351611 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:351611 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:351611 | pubmed:month | Jun | lld:pubmed |
pubmed-article:351611 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:351611 | pubmed:author | pubmed-author:SeebergEE | lld:pubmed |
pubmed-article:351611 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:351611 | pubmed:volume | 75 | lld:pubmed |
pubmed-article:351611 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:351611 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:351611 | pubmed:pagination | 2569-73 | lld:pubmed |
pubmed-article:351611 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:351611 | pubmed:year | 1978 | lld:pubmed |
pubmed-article:351611 | pubmed:articleTitle | Reconstitution of an Escherichia coli repair endonuclease activity from the separated uvrA+ and uvrB+/uvrC+ gene products. | lld:pubmed |
pubmed-article:351611 | pubmed:publicationType | Journal Article | lld:pubmed |
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