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. 1988 Aug 1;253(3):923–926. doi: 10.1042/bj2530923

Preferential ADP-ribosylation of arginine-3 in synthetic heptapeptide Leu-Arg-Arg-Ala-Ser-Leu-Gly.

R Matsuura 1, Y Tanigawa 1, M Tsuchiya 1, K Mishima 1, Y Yoshimura 1, M Shimoyama 1
PMCID: PMC1149392  PMID: 3140792

Abstract

Hen liver nuclear ADP-ribosyltransferase modified the synthetic heptapeptide Kemptide (Leu-Arg-Arg-Ala-Ser-Leu-Gly) at arginine-2 and/or arginine-3. Trypsin treatment of ADP-ribosyl-Kemptide revealed that the ADP-ribosylation of arginine-3 was constantly more abundant than that of arginine-2. ADP-ribosylation of Kemptide suppressed the subsequent phosphorylation by cyclic AMP-dependent protein kinase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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