TY - JOUR
T1 - Capillary affinity electrophoresis using lectins for the analysis of milk oligosaccharide structure and its application to bovine colostrum oligosaccharides
AU - Nakajima, Kazuki
AU - Kinoshita, Mitsuhiro
AU - Matsushita, Namiko
AU - Urashima, Tadasu
AU - Suzuki, Minoru
AU - Suzuki, Akemi
AU - Kakehi, Kazuaki
N1 - Funding Information:
We thank Professor T. Tsubota, University of Gifu, Dr. T. Komatsu, Ani Institute of the Japanese Black Bear, Dr. A.T. Derocher, University of Alberta, and Dr. O. Wiig, University of Oslo, for providing bear milk. This work was partly supported by the New Energy and Industrial Technology Organization.
PY - 2006/1/1
Y1 - 2006/1/1
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/29144475775
UR - https://www.scopus.com/pages/publications/29144475775#tab=citedBy
U2 - 10.1016/j.ab.2005.10.010
DO - 10.1016/j.ab.2005.10.010
M3 - Article
C2 - 16289347
AN - SCOPUS:29144475775
SN - 0003-2697
VL - 348
SP - 105
EP - 114
JO - Analytical Biochemistry
JF - Analytical Biochemistry
IS - 1
ER -