Abstract
The reactivity of alpha-amino groups of basic proteins towards fluorescamine is essentially abolished if salt linkages with DNA phosphate groups are formed. This observation prompted the elaboration of a very general assay which allows the determination of binding parameters for the interaction of proteins with DNA and chromatin. Protamines, labeled with fluorescamine prior to their binding by DNA appear to be useful probes to monitor the formation and nature of DNA-protein complexes.
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Selected References
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- Ando T., Watanabe S. A new method for fractionation of protamines and the amino acid sequences of salmine and three components of iridine. Int J Protein Res. 1969;1(3):221–224. doi: 10.1111/j.1399-3011.1969.tb01646.x. [DOI] [PubMed] [Google Scholar]
- Blow D. M., Steitz T. A. X-ray diffraction studies of enzymes. Annu Rev Biochem. 1970;39:63–100. doi: 10.1146/annurev.bi.39.070170.000431. [DOI] [PubMed] [Google Scholar]
- Bode J., Wagner K. G. The use of subunit exchange chromatography for the group specific fractionation of histones. Biochem Biophys Res Commun. 1975 Feb 17;62(4):868–876. doi: 10.1016/0006-291x(75)90403-9. [DOI] [PubMed] [Google Scholar]
- Burton D. R., Hyde J. E., Walker I. O. Histones F2a1 and F3 interact reversibly and cooperatively with DNA to form an equimolar complex in chromatin. FEBS Lett. 1975 Jul 15;55(1):77–80. doi: 10.1016/0014-5793(75)80962-8. [DOI] [PubMed] [Google Scholar]
- De Bernardo S., Weigele M., Toome V., Manhart K., Leimgruber W., Böhlen P., Stein S., Udenfriend S. Studies on the reaction of fluorescamine with primary amines. Arch Biochem Biophys. 1974 Jul;163(1):390–399. doi: 10.1016/0003-9861(74)90490-1. [DOI] [PubMed] [Google Scholar]
- Evans K., Konigsberg P., Cole R. D. Displacement of histones from deoxynucleoprotein by protamine. Arch Biochem Biophys. 1970 Nov;141(1):389–392. doi: 10.1016/0003-9861(70)90152-9. [DOI] [PubMed] [Google Scholar]
- Inoue S., Ando T. Interaction of clupeine with deoxyrinonucleic acid. I. Thermal melting and sedimentation studies. Biochemistry. 1970 Jan 20;9(2):388–394. doi: 10.1021/bi00804a027. [DOI] [PubMed] [Google Scholar]
- Johns E. W. Studies on histones. 7. Preparative methods for histone fractions from calf thymus. Biochem J. 1964 Jul;92(1):55–59. doi: 10.1042/bj0920055. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Louie A. J., Dixon G. H. Enzymatic modifications of the protamines. II. Separation and characterization of phosphorylated species of protamines from trout testis. Can J Biochem. 1974 Jun;52(6):536–546. doi: 10.1139/o74-078. [DOI] [PubMed] [Google Scholar]
- Malchy B., Kaplan H. Reactive properties of the amino groups of histones in calf thymus chromatin. J Mol Biol. 1974 Feb 5;82(4):537–545. doi: 10.1016/0022-2836(74)90247-2. [DOI] [PubMed] [Google Scholar]
- Marushige K., Dixon G. H. Transformation of trout testis chromatin. J Biol Chem. 1971 Sep 25;246(18):5799–5805. [PubMed] [Google Scholar]
- Means G. E., Feeney R. E. Reductive alkylation of amino groups in proteins. Biochemistry. 1968 Jun;7(6):2192–2201. doi: 10.1021/bi00846a023. [DOI] [PubMed] [Google Scholar]
- Simpson R. T. Modification of chromatin with acetic anhydride. Biochemistry. 1971 Nov 23;10(24):4466–4470. doi: 10.1021/bi00800a018. [DOI] [PubMed] [Google Scholar]
- Stein S., Böhlen P., Udenfriend S. Studies on the kinetics of reaction and hydrolysis of fluorescamine. Arch Biochem Biophys. 1974 Jul;163(1):400–403. doi: 10.1016/0003-9861(74)90491-3. [DOI] [PubMed] [Google Scholar]
- Wong T. K., Marushige K. Modification of histone binding in calf thymus chromatin by protamine. Biochemistry. 1975 Jan 14;14(1):122–127. doi: 10.1021/bi00672a021. [DOI] [PubMed] [Google Scholar]
- Yu S. S., Li H. J. Helix-coil transition and conformational studies of protamine-DNA complexes. Biopolymers. 1973 Dec;12(12):2777–2788. doi: 10.1002/bip.1973.360121211. [DOI] [PubMed] [Google Scholar]