Prenylated proteins: synthesis of geranylgeranylcysteine and identification of this thioether amino acid as a component of proteins in CHO cells. | Zendy

William W. Epstein | Zendy; David C. Lever | Zendy; Hans C. Rilling | Zendy

Open Access

Prenylated proteins: synthesis of geranylgeranylcysteine and identification of this thioether amino acid as a component of proteins in CHO cells.

Author(s) -

William W. Epstein,

David C. Lever,

Hans C. Rilling

Publication year - 1990

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.87.19.7352

Subject(s) - thioether , prenylation , chemistry , residue (chemistry) , cysteine , amino acid , derivative (finance) , hydrolysis , biochemistry , amino acid residue , acid hydrolysis , enzyme , chromatography , organic chemistry , peptide sequence , financial economics , economics , gene

Prenylated proteins, labeled in the isoprenoid residue by growing CHO cells in medium containing [5-3H]mevalonate, were degraded by three different proteolytic procedures, enzymatic or alkaline hydrolysis as well as hydrazinolysis. The products thus obtained were analyzed by HPLC with chemically prepared all-trans-geranylgeranylcysteine as a standard. About 10% of the radioactive products released by each lytic procedure showed the same chromatographic properties as geranylgeranylcysteine. This verifies the earlier conclusion, based on less-direct evidence, that this thioether derivative of cysteine is a component of naturally occurring proteins. The finding of this modified amino acid as a product of hydrazinolysis indicates that it is a carboxyl-terminal amino acid and that it is not carboxyl-methylated.

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