Abstract
Milk fat globule membrane (MFGM) glycoproteins were prepared from bovine milk at different stages of early lactation. Western blot analyses using several lectins revealed that reactivity of MFGM glycoproteins, especially 47K and 80K bands, to soybean agglutinin (SBA) remarkably increased during the lactation, while no change was observed for Ricinus communis agglutinin-I (RCA-I) binding. Sialidase treatment of MFGM glycoproteins revealed that the number of SBA-positive bands and the amount of SBA-positive oligosaccharides in these bands are increased during the lactation. Since SBA binds N-acetylgalactosamine terminated oligosaccharides, the results indicated that N-acetylgalactosaminylation of bovine MFGM glycoproteins is stimulated during the lactation.
Published Version
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