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- W1517832441 abstract "Abstract A method was developed for isolation and purification of radioactive poly ADP-ribose formed by a nuclear enzyme from rat liver. The procedure involved: (a) Pronase digestion and phenol extraction, (b) pancreatic RNase and pancreatic DNase digestion, (c) a first gel filtration through a Sephadex G-50 column, (d) micrococcal nuclease and spleen phosphodiesterase digestion, and (e) a second gel filtration. The over-all recovery of acid-insoluble radioactivity in the procedure was more than 50% and one-third of the acid-insoluble radioactivity was eluted just after the void volume from the Sephadex G-50 column. Increase of the specific radioactivity (counts per min per OD260) and decrease of the ratio of absorption at 280 mµ to that at 260 mµ were used as criteria of purity of poly ADP-ribose. At the final step of purification, the specific radioactivity of poly ADP-ribose was 80-fold that of the crude extract after Pronase digestion and phenol extraction. The specific activity of purified poly ADP-ribose and that of α-32P-ATP used as a precursor were 1.26 x 105 cpm per OD260 and 0.99 x 105 cpm per OD260, respectively. The A280:A260 ratio of absorption of purified poly ADP-ribose at the final step was 0.26. Purified poly ADP-ribose was completely hydrolyzed by snake venom phosphodiesterase and did not yield any nucleotide other than 5'-AMP and PR-AMP on Dowex 1 column chromatography. Experiments with 14C-ATP and NMN with a 32P-labeled whole nuclear preparation showed that poly ADP-ribose after the second gel filtration was devoid of 32P radioactivity. This indicates that poly ADP-ribose at this step was already free from contaminating RNA and DNA." @default.
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- W1517832441 date "1970-03-01" @default.
- W1517832441 modified "2023-09-30" @default.
- W1517832441 title "Studies on Poly Adenosine Diphosphate-Ribose" @default.
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- W1517832441 doi "https://doi.org/10.1016/s0021-9258(18)63239-9" @default.
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