|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2
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|
pubmed:dateCreated |
1981-12-15
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|
pubmed:abstractText |
The interaction of the antibiotic netropsin with calf thymus DNA, T4 DNA and poly(dA-dT) . poly(dA-dT) in complexes with sequential polypeptides containing repetitive lysine sequences and histone H1 was investigated using circular dichroism spectroscopy and equilibrium dialysis. Both soluble DNA-polypeptide complexes and insoluble complexes showed binding of netropsin. The possibility of displacement of polypeptides from DNA binding sites by competition with netropsin molecules was eliminated by experiments using 14C-labelled polypeptides. From the analysis of CD titration behavior as well as from the results of equilibrium dialysis studies it follows that netropsin does not compete with polypeptides for DNA binding sites, which suggests that these two ligands occupy different sites. Various explanations for minor differences in the CD behavior of the bound netropsin in the saturation region are also discussed.
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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
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|
pubmed:month |
Jul
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|
pubmed:issn |
0006-3002
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|
pubmed:author |
|
|
pubmed:issnType |
Print
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|
pubmed:day |
27
|
|
pubmed:volume |
654
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
175-80
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|
pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:6269619-Amino Acid Sequence,
pubmed-meshheading:6269619-Animals,
pubmed-meshheading:6269619-Binding Sites,
pubmed-meshheading:6269619-Cattle,
pubmed-meshheading:6269619-Circular Dichroism,
pubmed-meshheading:6269619-DNA,
pubmed-meshheading:6269619-DNA, Viral,
pubmed-meshheading:6269619-Guanidines,
pubmed-meshheading:6269619-Histones,
pubmed-meshheading:6269619-Lysine,
pubmed-meshheading:6269619-Netropsin,
pubmed-meshheading:6269619-Peptides,
pubmed-meshheading:6269619-Poly dA-dT
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|
pubmed:year |
1981
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|
pubmed:articleTitle |
Binding of netropsin to DNA in complexes with polypeptides containing repetitive lysine sequences.
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|
pubmed:publicationType |
Journal Article,
In Vitro
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