| Autor: |
Epstein WW; Department of Chemistry, University of Utah, Salt Lake City 84108., Lever DC, Rilling HC |
| Jazyk: |
angličtina |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 1990 Oct; Vol. 87 (19), pp. 7352-4. |
| DOI: |
10.1073/pnas.87.19.7352 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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