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A change in soybean agglutinin binding patterns of bovine milk fat globule membrane glycoproteins during early lactation
Author(s) -
Ujita Minoru,
Furukawa Kiyoshi,
Aoki Naohito,
Sato Takeshi,
Noda Akihiro,
Nakamura Ryo,
Greenwalt Dale E.,
Matsuda Tsukasa
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80496-h
Subject(s) - lactation , glycoprotein , soybean agglutinin , biochemistry , ricinus , chemistry , agglutinin , lectin , western blot , biology , gene , pregnancy , genetics
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.