PMID: 9348Apr 1, 1976

Poly(adenosine diphosphate ribose) is covalently linked to nuclear proteins by two types of bonds

Hoppe-Seyler's Zeitschrift für physiologische Chemie
P Adamietz, H Hilz


(ADP-ribose)n residues formed by short-term incubation of adult rat liver and Ehrlich carcinoma nuclei with labeled NAD were analyzed by Cs2SO4/guanidinium chloride/urea density gradient centrifugation. Comparison with samples in which the protein had been completely digested revealed that most, or probably all, acid-insoluble (ADP-ribose)n chains are covalently bound to nuclear proteins, as is true for the short, acid-soluble (ADP-ribose)n chains. Complete release of (ADP-ribose)n chains is effected by dilute alkali. In contrast, NH2OH liberated only part of the long and the short (ADP-ribose)n residues from the protein conjugates, indicating two types of bonds, both alkali-labile, but only one susceptible to neutral hydroxylamine. Both types of bonds were equally distributed among acid-soluble and acid-insoluble (ADP-ribose)n chains. -Stability of the (ADP-ribose)n protein conjugates during isolation is only guaranteed at pH values below 7.


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Related Concepts

Carcinoma, Ehrlich Tumor
Cell Nucleus
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