TY - JOUR
T1 - Interactions of concanavalin a with a trimannosyl oligosaccharide fragment of complex and high mannose type glycopeptides
AU - Brewer, Fred
AU - Bhattacharyya, Lokesh
AU - Brown, Rodney D.
AU - Koenig, Seymour H.
N1 - Funding Information:
The authors wishes to thank Dr. Jorgen Lonngren, Pharmacia Fine Chemicals, Uppsala, Sweden, and Mr. Martin Harldsson, University of Stockholm, for generous gifts of the synthetic trimannosyl oligosaccharide and hepta. This work was supported, in part, by Grant CA-\]6054 from the National Cancer Institute, Department of Health, Education, and Welfare, and Core Grant P30 CA-13330 from the same agency.
PY - 1985/3/29
Y1 - 1985/3/29
N2 - It has previously been reported that the binding interactions of concanavalin A with a purified high mannose type glycopeptide from ovalbumin differs from that with simple mono- and oligosaccharides (Brewer, C.F. (1979) Biochem. Biophys. Res. Commun. 90, 117-122). We now report studies with a synthetic analog of complex type glycopeptides, and a synthetic trimannosyl oligosaccharides fragment that is common to both complex and high mannose type glycopeptides. We find that both synthetic oligosaccharides undergo similar interactions with concanavalin A which mimic the effects of binding corresponding larger glycopeptides. Furthermore, the relative affinity of the trimannosyl oligosaccharides is 130-fold greater than the binding of methyl-α-D-mannopyranoside. The results indicate that the trimannosyl oligosaccharide is a unique structural element recognized by the lectin.
AB - It has previously been reported that the binding interactions of concanavalin A with a purified high mannose type glycopeptide from ovalbumin differs from that with simple mono- and oligosaccharides (Brewer, C.F. (1979) Biochem. Biophys. Res. Commun. 90, 117-122). We now report studies with a synthetic analog of complex type glycopeptides, and a synthetic trimannosyl oligosaccharides fragment that is common to both complex and high mannose type glycopeptides. We find that both synthetic oligosaccharides undergo similar interactions with concanavalin A which mimic the effects of binding corresponding larger glycopeptides. Furthermore, the relative affinity of the trimannosyl oligosaccharides is 130-fold greater than the binding of methyl-α-D-mannopyranoside. The results indicate that the trimannosyl oligosaccharide is a unique structural element recognized by the lectin.
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U2 - 10.1016/S0006-291X(85)80053-X
DO - 10.1016/S0006-291X(85)80053-X
M3 - Article
C2 - 3838666
AN - SCOPUS:0021885524
SN - 0006-291X
VL - 127
SP - 1066
EP - 1071
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -