[3H]Allicin: preparation and applications
| Autor: | Talia Miron, Aharon Rabinkov, T Bercovici, David Mirelman, Meir Wilchek |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
chemistry.chemical_classification
Allicin biology Biophysics Sulfoxide Cell Biology Alliin Sulfinic Acids Tritium Biochemistry Combinatorial chemistry chemistry.chemical_compound Enzyme chemistry Alliinase Chromatography Gel biology.protein Organic chemistry Adsorption Disulfides Molecular Biology Cysteine |
| Zdroj: | Analytical Biochemistry. 331:364-369 |
| ISSN: | 0003-2697 |
| DOI: | 10.1016/j.ab.2004.03.054 |
| Popis: | Allicin (diallylthiosulfinate), the active substance of garlic, has been shown to possess a variety of biological activities. Mechanistic and pharmacokinetic studies of allicin and its derivatives raise the need for a labeled compound. However, labeling of this volatile and unstable liquid requires delicate handling. Here, we describe a simple method for the preparation of (3)H-labeled allicin. This was achieved by applying synthetic [(3)H]alliin ([2,3-(3)H]allylcysteine sulfoxide) to a column containing immobilized alliinase [EC 4.1.1.4.] from garlic. Purification of [(3)H]allicin was done by differential adsorbtion of the reaction components on a neutral polystyrene resin, Porapak Q. Thiol-containing compounds are known to be the main target of allicin. In this work we demonstrated that [(3)H]allicin can be used for the synthesis of labeled [(3)H]allylmercapto derivatives of SH peptides and proteins. Thus, we prepared [(3)H]S-allylmercaptoglutathione which can be used in metabolic studies. Moreover, we showed that incubation of alliinase with [(3)H]allicin led to modification of 1.4 cysteine residues per subunit of the enzyme. |
| Databáze: | OpenAIRE |
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