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- W1528377984 abstract "The ADP-ribosylation of nonhistone, high mobility group (HMG) proteins in intact cultured cells was investigated. Radioactively labeled adenosine was used as a precursor to detect (ADP-ribose)n on protein. A protein fraction enriched in HMG proteins and histone H1 was separated from RNA and DNA by CsCl density gradient centrifugation, 5% perchloric acid extraction, and CM-Sephadex C-50 column chromatography. Poly- and mono(ADP-ribose) were recovered following alkaline hydrolysis, and 5'-AMP and (2'-(5-phosphoribosyl)-5'-AMP) were produced by phosphodiesterase treatment, indicating that the protein-bound radioactive material was (ADP-ribose)n. An average chain length of 1.5 to 1.8 was determined. Analysis of proteins by sodium dodecyl sulfate and acetic acid/urea polyacrylamide gel electrophoresis demonstrated that HMG 1, 2, 14, and 17 as well as histone H1 contained (ADP-ribose)n. Treatment of cells with 3-aminobenzamide, an inhibitor of (ADP-ribose)n synthetase, decreased endogenous ADP-ribosylation in both types of chromosomal proteins but that of HMG 14 and 17 was affected more." @default.
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- W1528377984 date "1983-04-01" @default.
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- W1528377984 title "ADP-ribosylation of nonhistone high mobility group proteins in intact cells." @default.
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- W1528377984 doi "https://doi.org/10.1016/s0021-9258(18)32583-3" @default.
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