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ECB-ART-32258
Biochem J 1985 Jan 15;2252:429-34. doi: 10.1042/bj2250429.
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ADP-ribosyltransferase in isolated nuclei from sea-urchin embryos.

Isoai A , Yasumasu I .


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The activity of ADP-ribosyltransferase in nuclei isolated from sea-urchin embryos was estimated by the incorporation of [adenosine-14C]NAD+ into the acid-insoluble fraction. Hydrolysis of this acid-insoluble product by snake venom phosphodiesterase yielded radioactive 5''-AMP and phosphoribosyl-AMP. The incorporation of [14C]-NAD+ was inhibited by 3-aminobenzamide and nicotinamide, potent inhibitors of ADP-ribosyltransferase. [14C]NAD+ incorporation into the acid-insoluble fraction results from the reaction of ADP-ribosyltransferase. The optimum pH for the enzyme in isolated nuclei was 7.5. The enzyme, in 50 mM-Tris/HCl buffer, pH 7.5, containing 0.5 mM-NAD+ and 0.5 mM-dithiothreitol, exhibited the highest activity at 18 degrees C in the presence of 14 mM-MgCl2. The apparent Km value for NAD+ was 25 microM. The activity of the enzyme was measured in nuclei isolated from the embryos at several stages during early development. The activity was maximum at the 16-32-cell stage and then decreased to a minimum at the mesenchyme blastula stage. Thereafter its activity slightly increased at the onset of gastrulation and decreased again at the prism stage.

???displayArticle.pubmedLink??? 2983674
???displayArticle.pmcLink??? PMC1144607
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Genes referenced: LOC100887844 LOC115919910

References [+] :
Adamietz, Rapid determination of chain length pattern in poly (ADP-ribose) samples. 1978, Pubmed