Receptor Proteins for Concanavalin A and Wheat Germ Agglutinin of Bovine Milk Fat Globule Membrane Probed by Affinity Chromatography in the Presence of Sodium Dodecyl Sulfate(Biological Chemistry)

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The receptor proteins for lectins of bovine milk fat globule membrane were probed by affinity chromatography on Concanavalin A (Con A)-and wheat germ agglutinin (WGA)-Sepharose in the presence of sodium dodecyl sulfate. Affinity chromatography on lectin column distinguished minor differences of specificity for lectin in a glycoprotein having the same mobility on electrophoresis. Of seven major glycoproteins (PAS-1 to 7), PAS-1 and -2 were bound to both Con A and WGA. Most of PAS-3 was retained on Con A. PAS-4 was retained on both WGA and Con A. A striking difference was observed between PAS-6 and -7 glycoproteins in the affinity to Con A, that is. PAS-6 was bound to Con A while PAS-7 not retained on Con A. However, most of PAS-6 and -7 was not retained on WGA, Part of PAS-5 was bound firmly while other parts failed to bind to both Con A and WGA. Our results suggest that the structure of saccharide chains of hte glycoproteins of MFGM is very complicated.
社団法人日本農芸化学会の論文
1986-12-23