Quantitation of prenylcysteines by a selective cleavage reaction
Autor: | Eveline Bruenger, L.M. Leining, William W. Epstein, Hans C. Rilling, David C. Lever |
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Rok vydání: | 1991 |
Předmět: |
Mevalonic Acid
CHO Cells Naphthols medicine.disease_cause chemistry.chemical_compound Mice Prenylation Thioether Cricetinae medicine Animals Humans Cysteine Escherichia coli Chromatography High Pressure Liquid chemistry.chemical_classification Multidisciplinary 3T3 Cells Yeast Terpenoid Amino acid chemistry Biochemistry Diterpenes Quantitative analysis (chemistry) Protein Processing Post-Translational HeLa Cells Research Article |
Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 88(21) |
ISSN: | 0027-8424 |
Popis: | The allylic thioether bond of the prenylcysteines of prenylated proteins has been shown to be cleaved by 2-naphthol under alkaline conditions to yield substituted naphthopyrans. These products are readily resolved from interfering materials by HPLC and have a strongly absorbing chromophore. Thus, this reaction is suitable for quantitative analysis of prenyl substituents of proteins, and we have examined a number of tissues for their content of prenylcysteines. These amino acids are present in mammalian tissues at a concentration of 0.36-1.4 nmol/mg of protein, with a ratio of geranylgeranylcysteine to farnesylcysteine in the range of 4 to 10. Prenylcysteines were also found in the cytosolic fraction of two mouse tissues at about one-third the concentration of the whole organ. The level of these modified amino acids was found to be significantly less in a yeast, a fungus, a brown alga, a higher plant, and an insect. Again, geranylgeranylcysteine is predominant. Prenylcysteines were absent from Escherichia coli but present in an archaebacterium. The prenylcysteine content of mammalian tissue is about 1% of that of cholesterol and about equal to that of ubiquinones and dolichols. Calculations indicate that about 0.5% of all proteins are prenylated. |
Databáze: | OpenAIRE |
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