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Poly(ADP-ribosylation) in Ascaris suum.

Authors
  • Walter, R D
  • Ossikovski, E
Type
Published Article
Journal
Hoppe-Seyler's Zeitschrift fur physiologische Chemie
Publication Date
Jul 01, 1984
Volume
365
Issue
7
Pages
805–808
Identifiers
PMID: 6090302
Source
Medline
Language
English
License
Unknown

Abstract

Poly(ADP-ribosylation) was demonstrated in the intestinal parasite Ascaris suum, especially in the reproductive tissues. The activity of the ADP-ribosyltransferase was found to depend on divalent cations and to be stimulated by deoxyribonuclease I about 5-fold. The reaction rate was optimal at a temperature of 30 degrees C and at pH about 8.4. The apparent Km value for NAD was estimated to be 0.2mM. The enzyme activity was effectively inhibited by nicotinamide (Ki = 65 microM) benzamide (6 microM), 3-aminobenzamide (10 microM), theophylline (35 microM) and thymidine (50 microM). The type of inhibition by these compounds was found to be competitive with respect to NAD.

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