RESUMEN
The objective of this study was to analyze the origin of proteins of a Chardonnay wine. Three various polyclonal antibodies raised against must, yeast, and bacteria proteins were produced. For microorganisms, only the secreted macromolecules were used. To this end, yeast and bacteria were cultured in a model medium under conditions close to those of winemaking. Results obtained using these specific antibodies indicate that most of the wine proteins came from grapes and many of them were glycoproteins. Some proteins of this Chardonnay wine came from the yeast; they were released during the alcoholic fermentation and consisted of high molecular weight mannoproteins. In contrast, no bacteria proteins were detected in this Chardonnay wine.
Asunto(s)
Proteínas Fúngicas/aislamiento & purificación , Proteínas de Plantas/aislamiento & purificación , Saccharomyces/química , Vitis/química , Vino/análisis , Animales , Especificidad de Anticuerpos , Proteínas Bacterianas/inmunología , Proteínas Bacterianas/aislamiento & purificación , Electroforesis en Gel de Poliacrilamida , Femenino , Proteínas Fúngicas/inmunología , Glicoproteínas/inmunología , Glicoproteínas/aislamiento & purificación , Sueros Inmunes/inmunología , Immunoblotting , Proteínas de Plantas/inmunología , Conejos , Vino/microbiologíaRESUMEN
A method was developed for the determination of putative lectin activities of cytokines. It involved the immunoblotting measurement of the quantity of these cytokines unbound to a series of different immobilized glycoconjugates and displacement of the bound cytokines with oligosaccharides of known structures. This method allows demonstrating that the following interleukins specifically recognize different oligosaccharide structures in a calcium-independent mechanism: interleukin-1alpha binds to the biantennary disialylated N-glycan completed with two Neu5Acalpha2-3 residues; interleukin-1beta to a GM4 sialylated glycolipid Neu5Acalpha2-3Galbeta1-Cer having very long and unusual long-chain bases; interleukin-4 to the 1,7 intramolecular lactone of N-acetyl-neuraminic acid; interleukin-6 to compounds having N-linked and O-linked HNK-1-like epitopes; and interleukin-7 to the sialyl-Tn antigen. Because the glycan ligands are rare structures in human circulating cells, it is suggested that such activities could be essential for providing specific signaling systems to cells having both the receptors and the oligosaccharide ligands of the interleukin at their cell surface.
