Characterization of concanavalin A sugar binding site by fluorine-19 nuclear magnetic resonance

Biochemistry ◽  
1974 ◽  
Vol 13 (19) ◽  
pp. 4038-4045 ◽  
Author(s):  
Gerald M. Alter ◽  
James A. Magnuson
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Binding Site ◽  
Concanavalin A ◽  
Sugar Binding ◽  
Nuclear Magnetic

Characterization by nuclear magnetic resonance of the concanavalin A binding oligosaccharide on the βb chain of placental β-hexosaminidase B: lectin binding to the separated polypeptide chains of hexosaminidases A and B

1985 ◽  
Vol 63 (7) ◽  
pp. 723-729 ◽  
Author(s):  
Brian F. O'dowd ◽  
Don Mahuran ◽  
Dale Cumming ◽  
J. Alexander Lowden
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Concanavalin A ◽  
Lectin Binding ◽  
Proton Nuclear Magnetic Resonance ◽  
Complex Type ◽  
High Mannose ◽  
Polypeptide Chains ◽  
Nuclear Magnetic

The type and distribution of the oligosaccharides on each polypeptide of human placental β-hexosaminidases A (α(βaβb)) and B (2((βaβb)) were examined. The denatured polypeptides were separated by isoelectric focussing in a polyacrylamide slab gel and each gel was then overlaid with 125I-labelled lectins. The study indicated that the βa chain contains negligible carbohydrate, the βb chain contains both the high-mannose and a complex type oligosaccharide, and the α chain contains predominantly high-mannose or hybrid type moieties. Two asparagine-linked high-mannose type oligosaccharides present on the βb polypeptide of β-hexosaminidase B were isolated by concanavalin A chromatography and by reverse-phase high pressure liquid chromatography. Proton nuclear magnetic resonance characterization of the oligosaccharides revealed an equimolar glycan mixture of the high-mannose type structure Man5 and Man6.

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