Literature DB >> 3011098

Reversible inactivation of ribonucleases by ADPribosylation.

E Leone, B Farina, M R Faraone Mennella.   

Abstract

The activity of purified bovine seminal RNAase and pancreatic RNAase A (EC 3.1.27.5) has been investigated following in vitro ADPribosylation in the presence of nuclear ADPribosyltransferase (EC 2.4.2.30) and NAD+ X ADPribosylation of these enzymes was correlated with a significant decrease in their activities. Approximately three residues of ADPribose were present per mol of enzyme. Removal of the bound ADPribose restored enzyme activity to near normal levels. Similar results were obtained with nuclei isolated from bull seminal vesicles as an endogenous source of seminal RNAase and nuclear ADPribosyltransferase. The findings suggest that in vitro ADPribosylation has a reversible inactivating effect on ribonucleases.

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Year:  1986        PMID: 3011098     DOI: 10.1016/0167-4838(86)90172-x

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  1 in total

1.  In vitro inhibition of HeLa cell nuclear ribonucleases by ADP-ribosylation.

Authors:  P Quesada; M Merola; B Farina; E Leone
Journal:  Mol Cell Biochem       Date:  1990-04-18       Impact factor: 3.396

  1 in total

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