
Primary structure of a new tetraantennary glycan of the N ‐acetyllactosaminic type isolated from human factor VIII/von Willebrand factor
Author(s) -
SAMOR Bruno,
MICHALSKI JeanClaude,
DEBRAY Henri,
MAZURIER Claudine,
GOUDEMAND Maurice,
HALBEEK Hermann,
VLIEGENTHART Johannes F. G.,
MONTREUIL Jean
Publication year - 1986
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1986.tb09750.x
Subject(s) - concanavalin a , chemistry , glycan , affinity chromatography , sepharose , von willebrand factor , glycopeptide , chromatography , biochemistry , glycoprotein , biology , immunology , platelet , enzyme , in vitro , antibiotics
N ‐Glycosidically linked glycopeptides released by mild alkaline treatment of human factor VIII/von Willebrand factor (FVIII/vWF) were fractionated by serial affinity chromatography on columns of Sepharose linked to concanavalin A (ConA) and Lens culinaris agglutinin (LCA). The fraction which is not retained on ConA‐Sepharose, but eluted from LCA‐Sepharose contains a pure minor glycopeptide which was structurally analysed. Based on the results of methylation analysis and 500‐MHz 1 H‐NMR spectroscopy, the following structure is proposed: