[Thermal denaturation and nuclease degradation of complexes of stellins A and B with DNA].
Identifieur interne : 000822 ( Ncbi/Curation ); précédent : 000821; suivant : 000823[Thermal denaturation and nuclease degradation of complexes of stellins A and B with DNA].
Auteurs : V K Rybin ; E P IulikovaSource :
- Biokhimiia (Moscow, Russia) [ 0320-9725 ] ; 1980.
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Abstract
The soluble complexes of stellins A and B-protamines from Acipenser stellatus-with DNA were obtained by direct mixing in 2,5.10(-4) M EDTA, pH 8,0. The differential curves of melting of the complexes reveal two transitions at Tmelt.1=49+/-1 degree and Tmelt.2=90+/-1 degree, corresponding to melting of DNA regions of free and protamine-bound DNA regions. The number of amino acid residues per one nucleotide in the protein-binding sites of DNA is 1,30 and 1,22 for the stellin A- and stellin B-DNA complexes, respectively. It was demonstrated that under denaturation the DNA filaments do not break apart completely. Data from the analysis of products of the complexes hydrolysis by DNAse I allowed to postulate a selective binding of the protamines to the AT-pairs of DNA. This assumption was confirmed by changes in the melting curves under different protein/DNA ratios.
PubMed: 6246979
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pubmed:6246979Le document en format XML
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<author><name sortKey="Iulikova, E P" sort="Iulikova, E P" uniqKey="Iulikova E" first="E P" last="Iulikova">E P Iulikova</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">[Thermal denaturation and nuclease degradation of complexes of stellins A and B with DNA].</title>
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<author><name sortKey="Iulikova, E P" sort="Iulikova, E P" uniqKey="Iulikova E" first="E P" last="Iulikova">E P Iulikova</name>
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<series><title level="j">Biokhimiia (Moscow, Russia)</title>
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<imprint><date when="1980" type="published">1980</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>DNA</term>
<term>Deoxyribonuclease I</term>
<term>Deoxyribonucleases</term>
<term>Endonucleases</term>
<term>Fish Proteins</term>
<term>Fishes</term>
<term>Kinetics</term>
<term>Nucleic Acid Denaturation</term>
<term>Protamines</term>
<term>Protein Binding</term>
<term>Temperature</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en"><term>DNA</term>
<term>Deoxyribonuclease I</term>
<term>Deoxyribonucleases</term>
<term>Endonucleases</term>
<term>Fish Proteins</term>
<term>Protamines</term>
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<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Fishes</term>
<term>Kinetics</term>
<term>Nucleic Acid Denaturation</term>
<term>Protein Binding</term>
<term>Temperature</term>
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<front><div type="abstract" xml:lang="en">The soluble complexes of stellins A and B-protamines from Acipenser stellatus-with DNA were obtained by direct mixing in 2,5.10(-4) M EDTA, pH 8,0. The differential curves of melting of the complexes reveal two transitions at Tmelt.1=49+/-1 degree and Tmelt.2=90+/-1 degree, corresponding to melting of DNA regions of free and protamine-bound DNA regions. The number of amino acid residues per one nucleotide in the protein-binding sites of DNA is 1,30 and 1,22 for the stellin A- and stellin B-DNA complexes, respectively. It was demonstrated that under denaturation the DNA filaments do not break apart completely. Data from the analysis of products of the complexes hydrolysis by DNAse I allowed to postulate a selective binding of the protamines to the AT-pairs of DNA. This assumption was confirmed by changes in the melting curves under different protein/DNA ratios.</div>
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