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The interaction of wheat germ agglutinin with keratan from cornea and nasal cartilage
Author(s) -
Carlsson Hans Erik,
Lönngren Jörgen,
Goldstein Irwin J.,
Christner James E.,
Jourdian George W.
Publication year - 1976
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(76)80011-7
Subject(s) - library science , medicine , chemistry , computer science
Wheat-germ agglutinin (WGA), a lectin isolated from Trit icum vulgaris, is widely used as a probe for studying carbohydrates found on the surfaces of malignant cells [1,2]. The agglutinin consists of two identical polypeptide chains. Each chain is reported to contain two identical binding sites, which can accomodate a N,N',N"-triacetyl chitotriosyl residue [ 1-7] ; internal (l~4)-N-acetyl-fl-D-glucosaminyl residues as well as terminal non-reducing N-acetyl-/3-D-glucosaminyl groups also interact with WGA [5,8,9]. Keratan sulfate, a connective tissue glycosaminoglycan, is composed of six to nine repeating disaccharide units of 4-O-/3-D-galactopyranosyl-N-acetyl-Dglucosamine [10,I 1]; the disaccharide units are glycosidically linked fl, 1-+3 [ 12,13 ]. Each of the carbohydrate residues contains varying amounts:of O-sulfate ester groups at carbon 6. The carbohydrate-binding specificity of WGA suggested that desulfated keratan sulfate should interact with WGA. The present communication documents the specific precipitation of desulfated keratan sulfate with WGA.