Abstract
Demembranized sperm and somatic nuclei of mammalian origin were extracted with high salt/urea/2-mercaptoethanol, treated with detergents and purified in CsCl density gradients to isolate DNA. Under these conditions a protein component still remained bound to DNA. This stable DNA-protein complex could be reduced to an oligodeoxynucleotide-peptide complex by extensive sequential digestions with DNase I and Pronase E. Chemical and enzymatic treatments of this complex indicated the presence of a phosphoester bond between DNA and a hydroxyamino acid. Two-dimensional tryptic peptide mapping revealed a remarkable similarity among the covalently linked protein components in all types of chromatin studied. These maps differed from the maps of mammalian topoisomerases I and II.
Original language | English (US) |
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Pages (from-to) | 437-440 |
Number of pages | 4 |
Journal | Journal of Molecular Biology |
Volume | 196 |
Issue number | 2 |
DOIs | |
State | Published - Jul 20 1987 |
Externally published | Yes |
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology