POLY(ADENOSINE DIPHOSPHORIBOSE) POLYMERASE-ACTIVITY AND ADENOSINE-DIPHOSPHATE RIBOSYLATION OF PROTEINS DURING PANCREATIC DEGENERATION AND REGENERATION

  • 1 January 1981
    • journal article
    • research article
    • Vol. 41  (4) , 1417-1421
Abstract
The activity of poly(adenosine diphosphoribose) polymerase in isolated rat pancreatic nuclei increased during pancreatic regeneration following ethionine treatment, although a possible relationship of enzyme activity to the initial degenerative phase may also be considered. There is a 2-fold increase in the enzyme activity during the destruction process which remains high during the regeneration period. This increase of activity observed during regeneration is not related to a decrease of the polymer degradation. The ADP ribosylation of proteins during pancreatic regeneration increased just before and during regeneration. The in vivo ADP ribosylation of nuclear proteins does not correlate with synthetase activity measured in nuclei during the degeneration period but does correlate during the regeneration period and thereafter with the relative amount of enzymatic activity found in nuclei. As verified by autoradiography, labeling of the nuclei by polyadenosine diphosphoribose polymer shows a marked increase during regeneration.

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