RESUMEN
Spectra of lectin-binding proteins of the human trophoblast were studied by the method affinity blotting using a set of loctins conjugated with peroxidase. The set included lectins Lens culinaris (LcL), Canavalia ensiformis (Con A), Ricinus communis (RCA 1), Arachis hypogaea (PNA), Triticum vulgaris (WGA), Laburnum anagyroides (LAL). Presence of N- and O-glycans in the composition of proteins of plasmatic membranes of a trophoblast was shown, partial characteristics of their oligosugar chains being presented. Sialic acids were established to be absent in the composition of alkaline phosphatase of mature placenta.
Asunto(s)
Lectinas/metabolismo , Proteínas de la Membrana/metabolismo , Trofoblastos/metabolismo , Ricinus communis , Concanavalina A/metabolismo , Humanos , Lectinas de Plantas , Plantas Tóxicas , Polisacáridos/química , Unión Proteica , Trofoblastos/ultraestructuraRESUMEN
This work was aimed to study the patterns of zein glycosylation. Zein proteins included 1-3% of sugars. The affinity of different lectins, such as concanavalin A (Con A), Lens culinaris lectin (LCL) and lectins of Arachis hypogaea (PNA), of Triticum vulgaris (WGA), of Dolichos biflorus (DBA), of Glycin max (SBA), of Lotus tetragonolobus (LTA), of Laburnum anagiroides (LAL), of Ricinus communis (RCA), of Phaseolus vulgaris (PHA) was used to analyze the glycosylation sites. All selected lectins interacted with zein proteins. It may serve a basis for determination of mannose, galactose, fucose and aminosugars. Some lectins were bound only by prolamines of some inbred lines, while others were connected with all lines.