Preliminary characterization of chelation-sensitive nucleoprotein particles

Nucleoprotein particles (B2), isolated following digestion of calf thymus chromatin with micrococcal nuclease, are resolved on a non-chelating Bio-Gel A-5m column. B2 protein electrophoresis showed the presence of several H1 species and several nonhistone proteins but was depleted in core histones....

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Veröffentlicht in:	Biochemical and biophysical research communications 1982-01, Vol.104 (2), p.491-499
Hauptverfasser:	Beary, David A., Vizard, Douglas L., LaBiche, Ronald A., Hardy, Kenneth J., Bryan, Sara E.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals calf thymus Cattle chromatin Chromatin - analysis Chromosomal Proteins, Non-Histone - isolation & purification Deoxyribonucleoproteins - isolation & purification DNA DNA - isolation & purification Edetic Acid Electrophoresis, Polyacrylamide Gel fractionation Histones - isolation & purification Micrococcal Nuclease Molecular Weight nucleoproteins Nucleoproteins - isolation & purification Thymus Gland - analysis
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Zusammenfassung:	Nucleoprotein particles (B2), isolated following digestion of calf thymus chromatin with micrococcal nuclease, are resolved on a non-chelating Bio-Gel A-5m column. B2 protein electrophoresis showed the presence of several H1 species and several nonhistone proteins but was depleted in core histones. DNA electrophoresis demonstrated that native B2 DNA has a length of about 46 base pairs. On DNA sequencing gels, the length distribution of denatured B2 DNA ranged from 12 to 35 bases with a weighted average chain length of about 26 bases. Depletion of a 20 base band in B2 DNA suggested specific protection of internucleosomal DNA sites during the nuclease digestion.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/0006-291X(82)90663-5