Abstract
Precisions are given on the fine specificity and on the usefulness of immobilized concanavalin A,Lens culinaris, Vicia faba andPisum sativum agglutinins for fractionation of glycopeptides with the N-glycosylamine linkage.
While insolubilized concanavalin A represents a very useful tool for the fractionation of both N-acetyllactosaminic and oligomannosidic type glycopeptides or related oligo-saccharides, immobilizedLens culinaris, as well asVicia faba orPisum sativum agglutinins allow the subfractionation of some N-acetyllactosaminic glycopeptide populations on the basis of the presence of an α-L-fucose residue substituting in C-6 position the N-acetylglucosamine residue involved in the N-glycosylamine bond.
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Abbreviations
- Con A:
-
Concanavalin A
- LCA:
-
Lens culinaris agglutinin
- VF A:
-
Vicia faba aggluti-nin
- PSA:
-
Pisum sativum agglutinin
- GP-h-STF:
-
glycopeptide isolated from human serotransferrin
- GP-h-LTF:
-
from human lactotransferrin
- GP-ovoTF:
-
hen ovotransferrin
- GP-b-LTF:
-
bovine lacto transferrin
- FNR:
-
non retained profile
- FR:
-
retained profile
- FE:
-
sharp elution profile
- FTB:
-
tightly bound profile
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Debray, H., Montreuil, J. Structural basis for the affinity of four insolubilized lectins, with a specificity for α-D-mannose, towards various glycopeptides with the N-glycosylamine linkage and related oligosaccharides. J Biosci 5 (Suppl 1), 93–100 (1983). https://doi.org/10.1007/BF02702979
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DOI: https://doi.org/10.1007/BF02702979