Stable DNA-protein complexes in eukaryotic chromatin.
J Mol Biol
; 196(2): 437-40, 1987 Jul 20.
Article
en En
| MEDLINE
| ID: mdl-3656455
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
ADN
/
Cromatina
/
Proteínas
/
Células
/
Células Eucariotas
Límite:
Animals
Idioma:
En
Revista:
J Mol Biol
Año:
1987
Tipo del documento:
Article
Pais de publicación:
Países Bajos