[Circular dichroism spectra of DNA complexes with stellins A and B--protamines from Acipenser stellatus].
Identifieur interne : 002266 ( Main/Merge ); précédent : 002265; suivant : 002267[Circular dichroism spectra of DNA complexes with stellins A and B--protamines from Acipenser stellatus].
Auteurs : V K Rybin ; E P KulikovaSource :
- Biokhimiia (Moscow, Russia) [ 0320-9725 ] ; 1981.
English descriptors
- KwdEn :
- MESH :
- chemical : DNA, Protamines.
- Animals, Circular Dichroism, Fishes, Nucleic Acid Conformation, Protein Conformation.
Abstract
The circular dichroism (CD) spectra of DNA complexes with stellins A and B, protamines from Acipenser stellatus, in 2,5 x 10(-4) M EDTA were studied. The CD spectrum of the stellin B--DNA complex practically coincides with that of original DNA. In the CD spectrum of the stellin A--DNA complex the positive band amplitude increases at 275 nm, while the negative band amplitude decreases at 245 nm at increasing of protein/DNA ratio. The resulting A-like CD spectrum is apparently coupled with the changes in the parameters of DNA double helix. The changes in the CD spectra in the stellin A--DNA complex are correlated with a higher capacity of stellin A for helix formation in ethanol. The data obtained suggest that individual components of stellin play a specific role in the structural organization of nucleoprotamine.
PubMed: 7248385
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pubmed:7248385Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en">[Circular dichroism spectra of DNA complexes with stellins A and B--protamines from Acipenser stellatus].</title>
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<term>Protamines</term>
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<front><div type="abstract" xml:lang="en">The circular dichroism (CD) spectra of DNA complexes with stellins A and B, protamines from Acipenser stellatus, in 2,5 x 10(-4) M EDTA were studied. The CD spectrum of the stellin B--DNA complex practically coincides with that of original DNA. In the CD spectrum of the stellin A--DNA complex the positive band amplitude increases at 275 nm, while the negative band amplitude decreases at 245 nm at increasing of protein/DNA ratio. The resulting A-like CD spectrum is apparently coupled with the changes in the parameters of DNA double helix. The changes in the CD spectra in the stellin A--DNA complex are correlated with a higher capacity of stellin A for helix formation in ethanol. The data obtained suggest that individual components of stellin play a specific role in the structural organization of nucleoprotamine.</div>
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