A change in soybean agglutinin binding patterns of bovine milk fat globule membrane glycoproteins during early lactation

FEBS Letters

Sato, Takeshi²  Noda, Akihiro¹  Furukawa, Kiyoshi²  Ujita, Minoru¹  Aoki, Naohito¹  Matsuda, Tsukasa¹  Greenwalt, Dale E.³  Nakamura, Ryo¹ 

[1] Department of Applied Biological Sciences, School of Agricultural Science, Nagoya University, Nagoya 464-01, Japan;Department of Biochemistry, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan;Holland Laboratory, American Red Cross, Rockville, MD 20855, USA

关键词: N-Linked sugar chains;    N-Acetylgalactosaminylation;    Sialylation;    Lactation;    CBB;    Coomassie Brilliant Blue;    MFGM;    milk fat globule membrane;    PVDF;    polyvinylidene difluoride;    RCA-I;    Ricinus communis agglutinin-I;    SBA;    soy-bean agglutinin;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;    WGA;    wheat germ agglutinin;   

DOI  :  10.1016/0014-5793(93)80496-H

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown