The Modification of Nuclear Proteins by ADP-ribosylation
Autor: | Alexander J. MacGILLIVRAY, William J. D. Whish, David Rickwood |
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Rok vydání: | 1977 |
Předmět: |
musculoskeletal diseases
Poly Adenosine Diphosphate Ribose Chromosomal Proteins Non-Histone Fractionation Biochemistry Cell Line Histones Mice chemistry.chemical_compound medicine Animals Nuclear protein Cell Nucleus biology Nucleoside Diphosphate Sugars Chemistry Brain NAD musculoskeletal system In vitro Cell nucleus medicine.anatomical_structure Histone Liver ADP-ribosylation biology.protein Urea NAD+ kinase |
Zdroj: | European Journal of Biochemistry. 79:589-598 |
ISSN: | 1432-1033 0014-2956 |
DOI: | 10.1111/j.1432-1033.1977.tb11843.x |
Popis: | When incubated in vitro purified mouse nuclei incorporate NAD into poly(ADP-Rib). Analysis of the product on CsDl/urea gradients showed that a large proportion of the poly(ADP-Rib) was not attached to protein. The free poly(ADP-Rib) did not appear to arise through degradation and its chain length was significantly longer than the poly(ADP-Rib) attached to proteins. Fractionation of the proteins on hydroxyapatite revealed that tissue-specific modification of both the histones and non-histone proteins, had occurred. In the case of one protein species there was evidence for the existence of several forms with different numbers of ADP-Rib residues. |
Databáze: | OpenAIRE |
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