异戊二烯化蛋白：蛋白质与半胱氨酸硫醚键的证明。

Prenylated proteins: demonstration of a thioether linkage to cysteine of proteins.

作者信息

Rilling H C, Bruenger E, Epstein W W, Kandutsch A A

机构信息

Department of Biochemistry, University of Utah School of Medicine, Salt Lake City.

出版信息

Biochem Biophys Res Commun. 1989 Aug 30;163(1):143-8. doi: 10.1016/0006-291x(89)92111-6.

DOI:10.1016/0006-291x(89)92111-6

PMID:2775255

Abstract

Prenylated amino acid fragments have been isolated from prenylated proteins of Chinese hamster ovary cells. Gel-exclusion chromatography indicates that these proteins are modified by two different prenyl groups. The prenyl-amino acid fragments are labeled by 35S from cysteine, and this bond is cleaved by Raney-Ni, proving that the prenyl residue is linked to protein via a thioether to cysteine. Hydrazinolysis has been used to demonstrate that the cysteine is carboxy terminal.

摘要

已从中国仓鼠卵巢细胞的异戊二烯化蛋白质中分离出异戊二烯化氨基酸片段。凝胶排阻色谱表明这些蛋白质被两种不同的异戊二烯基团修饰。异戊二烯化氨基酸片段由半胱氨酸的35S标记，并且该键可被雷尼镍裂解，证明异戊二烯残基通过硫醚与半胱氨酸连接至蛋白质。已使用肼解来证明半胱氨酸是羧基末端。