Binding of the basement-membrane glycoprotein laminin to glycosaminoglycans. An affinity-chromatography study

The binding of the basement-membrane glycoprotein laminin to glycosaminoglycans (aggregating and non-aggregating subsets of heparan sulphates and dermatan sulphates, as well as heparin, chondroitin sulphates and hyaluronic acid) was studied by affinity chromatography. Partially periodate-oxidized ch...

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Bibliographic Details
Published in:Biochemical journal 1981-12, Vol.199 (3), p.699-704
Main Authors: Del Rosso, M, Cappelletti, R, Viti, M, Vannucchi, S, Chiarugi, V
Format: Article
Language:English
Subjects:
Animals
Basement Membrane - metabolism
basement membranes
Binding, Competitive
Chromatography, Affinity
Glycoproteins - metabolism
glycosaminoglycans
Glycosaminoglycans - metabolism
Laminin
Membrane Proteins - metabolism
Mice
Protein Binding
Sepharose
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Summary:The binding of the basement-membrane glycoprotein laminin to glycosaminoglycans (aggregating and non-aggregating subsets of heparan sulphates and dermatan sulphates, as well as heparin, chondroitin sulphates and hyaluronic acid) was studied by affinity chromatography. Partially periodate-oxidized chains of glycosaminoglycans were coupled to adipic acid dihydrazide-substituted agarose. Co-polymeric glycosaminoglycans reveal high affinity for laminin, whereas hyaluronic acid does not. Competitive-release experiments indicate that glycosaminoglycans share a common binding site on the laminin molecule.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj1990699