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Purification of ADP-ribosylated nuclear proteins by covalent chromatography on dihydroxyboryl polyacrylamide beads and their characterization.

Nuclear proteins modified by mono or poly ADP-ribosylation were selectively isolated and purified by covalent chromatography on a dihydroxyboryl polyacrylamide bead column that specifically interacts with cis-diol-containing compounds. From rat liver nuclei that had been incubated with NAD+, histone...

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Bibliografiska uppgifter
Huvudupphovsmän: Okayama, H, Ueda, K, Hayaishi, O
Materialtyp: Artigo
Språk:Inglês
Publicerad: 1978
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Länkar:https://ncbi.nlm.nih.gov/pmc/articles/PMC411418/
https://ncbi.nlm.nih.gov/pubmed/274702
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