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Separation of disaccharides by affinity capillary electrophoresis in lectin‐containing electrophoretic solutions
Author(s) -
Taga Atsushi,
Yabusako Yukiko,
Kitano Atsuko,
Honda Susumu
Publication year - 1998
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150191513
Subject(s) - chemistry , melibiose , chromatography , lectin , capillary electrophoresis , electrophoresis , maltose , soybean agglutinin , affinity electrophoresis , agglutinin , affinity chromatography , biochemistry , sucrose , enzyme
Separation of the 1‐phenyl‐3‐methyl‐5‐pyrazolone (PMP) derivatives of simple disaccharides (maltose, cellobiose, gentiobiose, lactose, and melibiose) by affinity capillary electrophoresis was investigated using lectin‐containing neutral phosphate buffers, filled in a linear polyacrylamide‐coated capillary. When Lens culinaris agglutinin (LCA) was added, the derivatives of glucobioses were retarded with varying magnitudes depending on the amount of LCA and were well separated from each other and from galactosyl glucose under optimized conditions. Addition of Ricinus communis 60 kDa agglutinin (RCA 60 ) to the phosphate buffer gave a different migration profile, in which the derivatives of galactosyl glucoses were more retarded than those of glucobioses. However, addition of either lectin did not accomplish complete separation of the derivatives of all these disaccharides even under optimum conditions. The addition of two kinds of lectins in appropriate proportions improved separation. Thus, the binary system composed of LCA and RCA 60 , as well as LCA and soybean agglutinin from Glycine max (SBA), gave better separation of these derivatives, giving peak tops for all derivatives.