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合成七肽Leu-Arg-Arg-Ala-Ser-Leu-Gly中精氨酸-3的优先ADP核糖基化作用

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

作者信息

Matsuura R, Tanigawa Y, Tsuchiya M, Mishima K, Yoshimura Y, Shimoyama M

机构信息

Department of Biochemistry, Shimane Medical University, Izumo, Japan.

出版信息

Biochem J. 1988 Aug 1;253(3):923-6. doi: 10.1042/bj2530923.

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.

摘要

鸡肝细胞核 ADP-核糖基转移酶使合成的七肽肯普肽(Leu-Arg-Arg-Ala-Ser-Leu-Gly)的精氨酸-2 和/或精氨酸-3 发生修饰。用胰蛋白酶处理 ADP-核糖基化的肯普肽发现,精氨酸-3 的 ADP-核糖基化始终比精氨酸-2 的更为丰富。肯普肽的 ADP-核糖基化抑制了随后由环磷酸腺苷依赖性蛋白激酶介导的磷酸化作用。

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