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

The Biochemical journal ·Vol. 199 ·No. 3 ·1981-12-01 ·Pages 699-704

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

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.

MeSH Terms

Animals Basement Membrane/metabolism Binding, Competitive Chromatography, Affinity Glycoproteins/metabolism Glycosaminoglycans/metabolism Laminin Membrane Proteins/metabolism Mice Protein Binding Sepharose

Chemicals

Glycoproteins Glycosaminoglycans Laminin Membrane Proteins Sepharose

Authors & Affiliations

5 authors, click to expand affiliations / ORCID

Del Rosso M

Cappelletti R

Viti M

Vannucchi S

Chiarugi V

References (15)

15 references, click to expand

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Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1990699

Published

1981-12-01

Pages

699-704

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1163427

Subset

External Links

PubMed source DOI: 10.1042/bj1990699 PMC Full Text View journal details

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

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