Prenylated proteins: demonstration of a thioether linkage to cysteine of proteins.
Cell-Line, Cysteine, Ethers, Hamsters, Mevalonic-Acid: me, Protein-Processing-Post-Translational, Proteins, SUPPORT-NON-U-S-GOVT, SUPPORT-U-S-GOVT-P-H-S, Terpenes: me
Biochem Biophys Res Commun 1989 Aug 30;163(1):143-8
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.
Rilling, H C.; Bruenger, E; Epstein, W W.; and Kandutsch, A A., " Prenylated proteins: demonstration of a thioether linkage to cysteine of proteins." (1989). Faculty Research 1980 - 1989. 1156.
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