Co-operative binding of the globular domain of histone H5 to DNA

The globular domain of histone H5 (GH5) was prepared by trypsin digestion of H5 that was extracted from chicken erythrocyte nuclei with NaCl. Electron microscopy, sucrose gradient centrifugation, native agarose gel electrophoresis and equilibrium density gradient ultracentrifugation show that GH5 bi...

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Veröffentlicht in:	Journal of molecular biology 1992-06, Vol.225 (4), p.1105-1121
Hauptverfasser:	Draves, P.H., Lowary, P.T., Widom, J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites Biological and medical sciences Cell Nucleus - metabolism Centrifugation, Density Gradient Chickens chromatin Chromatin - metabolism co-operative binding DNA - isolation & purification DNA - metabolism DNA - ultrastructure Erythrocytes - metabolism Fundamental and applied biological sciences. Psychology GH5 histone H1 histone H5 Histones - isolation & purification Histones - metabolism Histones - ultrastructure Interactions. Associations Intermolecular phenomena Kinetics Light Microscopy, Electron Molecular biophysics Scattering, Radiation
Online-Zugang:	Volltext
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