Interaction between dermatan sulphate chains. I. Affinity chromatography of copolymeric galactosaminioglycans on dermatan sulphate-substituted agarose.

(1) Binding of copolymeric as well as homopolymeric galactosaminoblycan to dermatan sulphate-substituted gels has been demonstrated. Materials bound in the presence of 0.15 M NaC1 was eluted with either 1 M urea, 0.5 M guanidine - HC1 or 0.5 M NaC1. Homopolymeric galactosaminoglycans were also displaced by 0.5 M sodium acetate. The interaction was not dependent on divalent cations. (2) Dermatan sulphate has been fractionated into aggregating and nonaggregating species by gel chromatography in the presence of 0.5 M sodium acetate. In the presence of 3.1 M sodium acetate or 0.5 M guanidine - HC1 no aggregation was observed. (3) Crosslinks formed during periodate oxidation at physiological ionic strength have been ascribed to chain-chain interaction. (4) Chondroitin 4-sulphate, heparan sulphate and heparin also showed interaction with gels substituted with copolymeric galactosaminoglycans, while chondroitin 6-sulphate, hyaluronate and keratan sulphate did not. (5) Binding of copolymeric galactosaminoglycan chains to dermatan sulphate- or chondroitin sulphate-substituted gels was most pronounced when the copolymeric chains similar proportions of L-iduronic and D-glucuronic acid.