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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
20
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pubmed:dateCreated |
1987-8-13
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pubmed:abstractText |
A 58-kDa monomer of terminal transferase was isolated from calf thymus using a monoclonal antibody affinity column. The enzymatic activity was comparable to that of the 44-kDa alpha beta dimer isolated by conventional methods. Binding of the two enzyme forms to single-stranded DNA was monitored by fluorescence. The site size of both forms was approximately 11 +/- 2 nucleotides. Binding of the 44-kDa alpha beta dimer to polydeoxyadenosine was examined under several conditions. The cooperativity parameter increased from about 90 in the presence of Mg2+ to 300-400 in the absence of Mg2+. The observed dissociation constant of 3-5 microM was essentially independent of salt concentration, whereas the intrinsic dissociation constant decreased about 5-fold in the presence of Mg2+. The binding parameters of the 58-kDa monomer were independent of buffer composition and were similar to those of the 44-kDa alpha beta dimer in the presence of Mg2+. These results indicate that the additional 14-kDa peptide sequences present in the high molecular mass monomer form are not part of the DNA-binding site of terminal transferase.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Single-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Nucleotidylexotransferase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
262
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9494-502
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3597421-Animals,
pubmed-meshheading:3597421-Cattle,
pubmed-meshheading:3597421-Chromatography, Affinity,
pubmed-meshheading:3597421-DNA, Single-Stranded,
pubmed-meshheading:3597421-DNA Nucleotidylexotransferase,
pubmed-meshheading:3597421-DNA Nucleotidyltransferases,
pubmed-meshheading:3597421-Kinetics,
pubmed-meshheading:3597421-Macromolecular Substances,
pubmed-meshheading:3597421-Molecular Weight,
pubmed-meshheading:3597421-Thymus Gland
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pubmed:year |
1987
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pubmed:articleTitle |
Interaction of terminal transferase with single-stranded DNA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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