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...
Αποθηκεύτηκε σε:
| Εκδόθηκε σε: | Proc Natl Acad Sci U S A |
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| Κύριοι συγγραφείς: | , , |
| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
National Academy of Sciences
1978
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| Θέματα: | |
| Διαθέσιμο Online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC411418/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/274702/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.75.3.1111 |
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