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Literature DB >> 1250694

Cooperative binding of fluorescein-labeled clupeine by DNA.

Abstract

The alpha-amino group of clupeine fraction Z from herring sperm was coupled with fluorescein. Binding of the labeled protamine by DNA is accompanied by significant fluorescence quenching up to 80%. This allowed the convenient determination of the binding behavior of protamine and DNA. Binding was found to be strongly cooperative and not be significantly affected by the size of DNA. The ionic strength dependence in the range up to 0.3 M NaCl was rather small. Binding parameters were derived according to classical unique-site treatment and to a concept which includes vagrant multi-site binding.

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Year: 1976 PMID： 1250694 PMCID： PMC342884 DOI： 10.1093/nar/3.1.149

Source DB: PubMed Journal: Nucleic Acids Res ISSN： 0305-1048 Impact factor: 16.971

19 in total

1. Modification of histone binding in calf thymus chromatin by protamine.

Authors: T K Wong; K Marushige
Journal: Biochemistry Date: 1975-01-14 Impact factor: 3.162

2. Specifity of DNA-basic polypeptide interactions. Influence of neutral residues incorporated into polylysine and polyarginine.

Authors: K Wehling; H A Arfmann; K H Standke; K G Wagner
Journal: Nucleic Acids Res Date: 1975-06 Impact factor: 16.971

3. Application of fluorescamine to the study of protein-DNA interactions.

Authors: J Bode
Journal: Nucleic Acids Res Date: 1975-10 Impact factor: 16.971

4. Theoretical aspects of DNA-protein interactions: co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice.

Authors: J D McGhee; P H von Hippel
Journal: J Mol Biol Date: 1974-06-25 Impact factor: 5.469

Cooperative binding of fluorescein-labeled clupeine by DNA.

1. Modification of histone binding in calf thymus chromatin by protamine.

2. Specifity of DNA-basic polypeptide interactions. Influence of neutral residues incorporated into polylysine and polyarginine.

3. Application of fluorescamine to the study of protein-DNA interactions.

4. Theoretical aspects of DNA-protein interactions: co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice.

5. Helix-coil transition and conformational studies of protamine-DNA complexes.

6. A new method for fractionation of protamines and the amino acid sequences of salmine and three components of iridine.

7. On the structure and stability of DNA-protamine and DNA-polypeptide complexes.

8. Interaction of clupeine with deoxyrinonucleic acid. I. Thermal melting and sedimentation studies.

9. Interaction of clupeine with deoxyribonucleic acid. II. Optical rotatory dispersion studies.

10. Studies on histones. 7. Preparative methods for histone fractions from calf thymus.

1. Phosphorylated protamines. II. Circular dichroism of complexes with DNA, dependency on ionic strength.

2. Phosphorylated protamines. I. Binding stoichiometry and thermal stability of complexes in DNA.

3. The binding of protamines to DNA; role of protamine phosphorylation.