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 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.
D000818:Animals; D001485:Basement Membrane / Q000378:metabolism; D001667:Binding, Competitive; D002846:Chromatography, Affinity; D006023:Glycoproteins / Q000378:metabolism*; D006025:Glycosaminoglycans / Q000378:metabolism*; D007797:Laminin; D008565:Membrane Proteins / Q000378:metabolism*; D051379:Mice; D011485:Protein Binding; D012685:Sepharose
D006023:Glycoproteins; D006025:Glycosaminoglycans; D007797:Laminin; D008565:Membrane Proteins; D012685:Sepharose