Prenylated proteins: demonstration of a thioether linkage to cysteine of proteins.
Biochem Biophys Res Commun
; 163(1): 143-8, 1989 Aug 30.
Article
en En
| MEDLINE
| ID: mdl-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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Terpenos
/
Proteínas
/
Cisteína
/
Ácido Mevalónico
Límite:
Animals
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
1989
Tipo del documento:
Article