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. 1981 Dec 1;199(3):699-704.
doi: 10.1042/bj1990699.

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

M Del Rosso, R Cappelletti, M Viti, S Vannucchi, V Chiarugi

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

M Del Rosso et al. Biochem J. .

Abstract

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.

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