Capillary affinity electrophoresis using lectins for the analysis of milk oligosaccharide structure and its application to bovine colostrum oligosaccharides

Kazuki Nakajima, Mitsuhiro Kinoshita, Namiko Matsushita, Tadasu Urashima, Minoru Suzuki, Akemi Suzuki, Kazuaki Kakehi

研究成果: Article査読

37 被引用数 (Scopus)

抄録

Animal colostrum and milk contain complex mixtures of oligosaccharides, which have species-specific profiles. Milk oligosaccharides have various types of structure related to the core structures of glycolipids and N- and O-glycans of glycoproteins and provide a good library to examine the binding of oligosaccharides to various lectins. Recently, we reported a capillary affinity electrophoresis (CAE) method for analyzing the interactions between lectins and complex mixtures of N-linked oligosaccharides prepared from serum glycoproteins [K. Nakajima, Y. Oda, M. Kinoshita, K. Kakehi, J. Proteome Res. 2 (2003) 81-88]. The present paper reports the interactions between 24 milk oligosaccharides and six lectins (PA-I, RCA120, SBA, WGA, UEA-I, and AAL) analyzed using CAE. Based on the resulting data, we constructed a library that enables us to determine nonreducing terminal monosaccharides, such as Gal, GalNAc, GlcNAc, and Fuc, and to differentiate Gal- or Fuc-linked isomers, such as lacto-N-tetraose, lacto-N-neotetraose, and lacto-N-fucopentaose II and III. In addition, using the library, we show that a combination of the lectins can characterize the neutral oligosaccharides derived from bovine colostrum.

本文言語English
ページ(範囲)105-114
ページ数10
ジャーナルAnalytical Biochemistry
348
1
DOI
出版ステータスPublished - 01-01-2006
外部発表はい

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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