Faculty Research 1980 - 1989
Prenylated proteins: demonstration of a thioether linkage to cysteine of proteins.
Document Type
Article
Publication Date
1989
Keywords
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
First Page
143
Last Page
148
JAX Source
Biochem Biophys Res Commun 1989 Aug 30;163(1):143-8
Grant
GM38589
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.
Recommended Citation
Rilling HC,
Bruenger E,
Epstein WW,
Kandutsch AA.
Prenylated proteins: demonstration of a thioether linkage to cysteine of proteins. Biochem Biophys Res Commun 1989 Aug 30;163(1):143-8