TY - JOUR
T1 - Glycamine formation via reductive amination of oligosaccharides with benzylamine
AU - Yoshida, Tomoaki
N1 - Funding Information:
The authors acknowledge the technical assistance of Dr. Charles Cottrell and David Chang for performing NMR and FAB-MS services. Support for this work provided by National Institutes of Health Grants DK45742 and GM48048 (K.G.R) and by the Ohio State University Office of Research is gratefully acknowledged.
PY - 1994/1/1
Y1 - 1994/1/1
N2 - This chapter presents a more efficient method for producing glycamine by employing benzylamine as an amino donor. The higher efficiency of this method is because of the ease of Schiff base formation attributable to the lower basicity of benzylamine as well as to the lesser amount of dimeric by-product formed owing to the difficulty of tertiary amine formation. Although this approach requires an extra step of hydrogenolysis to unmask the amino group, the advantages outweigh the minor inconvenience. Although the chapter describes only two examples of oligosaccharide-glycamine formation, and coupling of one of the glycamines to ribonuclease A, the methodology established in the chapter should be applicable to many other oligosaccharide-protein combinations, including sialylated oligosaccharides.
AB - This chapter presents a more efficient method for producing glycamine by employing benzylamine as an amino donor. The higher efficiency of this method is because of the ease of Schiff base formation attributable to the lower basicity of benzylamine as well as to the lesser amount of dimeric by-product formed owing to the difficulty of tertiary amine formation. Although this approach requires an extra step of hydrogenolysis to unmask the amino group, the advantages outweigh the minor inconvenience. Although the chapter describes only two examples of oligosaccharide-glycamine formation, and coupling of one of the glycamines to ribonuclease A, the methodology established in the chapter should be applicable to many other oligosaccharide-protein combinations, including sialylated oligosaccharides.
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U2 - 10.1016/S0076-6879(94)47006-5
DO - 10.1016/S0076-6879(94)47006-5
M3 - Article
C2 - 7898370
AN - SCOPUS:0028673874
SN - 0076-6879
VL - 247
SP - 55
EP - 64
JO - Methods in Enzymology
JF - Methods in Enzymology
IS - C
ER -