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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1976-6-2
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pubmed:abstractText |
A DNA kinase has been partially purified from rat liver nuclei by a procedure which also yields DNA ligase. The kinase uses ATP to phosphorylate specifically the 5'-hydroxyl termini of oligodeoxynucleotides and of single- or double-stranded DNA, yielding 5'-phosphate termini and ADP. The kinase is inactive on RNA, or on oligodeoxynucleotides of chain length less than approximately 10 to 12 residues. The kinase requires a divalent cation (Mg2+, Mn2+, Co2+, Zn2+, Ni2+, or Ca2+) for activity and has an acidic pH optimum. It is inhibited by a variety of nucleotides as well as by very low levels of inorganic and organic sulfate compounds and sulfate analogues. The molecular weight of the kinase is estimated to be 8 times 10(4) from gel filtration.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
251
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1767-74
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3504-Animals,
pubmed-meshheading:3504-Cations, Divalent,
pubmed-meshheading:3504-Cations, Monovalent,
pubmed-meshheading:3504-Cell Nucleus,
pubmed-meshheading:3504-Hydrogen-Ion Concentration,
pubmed-meshheading:3504-Kinetics,
pubmed-meshheading:3504-Liver,
pubmed-meshheading:3504-Osmolar Concentration,
pubmed-meshheading:3504-Phosphotransferases,
pubmed-meshheading:3504-Polynucleotide 5'-Hydroxyl-Kinase,
pubmed-meshheading:3504-Rats
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pubmed:year |
1976
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pubmed:articleTitle |
A deoxyribonucleic acid kinase from nuclei of rat liver. Purification and properties.
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pubmed:publicationType |
Journal Article
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