Polyelectrolyte complexes. 2. Interaction between collagen and polyanions
1979; Elsevier BV; Volume: 1; Issue: 5 Linguagem: Inglês
10.1016/0141-8130(79)90016-3
ISSN1879-0003
AutoresR. B. Cundall, John B. Lawton, David R. Murray, G. O. Phillips,
Tópico(s)Osteoarthritis Treatment and Mechanisms
ResumoThe electrostatic interactions that occur in connective tissue between polyanions and proteins have been studied in model systems by a technique involving a fluorescent probe, acridine orange. It was found that collagen bound more strongly than bovine serum albumin to the polyanions studied. At pH 3.0, collagen formed strong complexes of definite stoichiometry with chondroitin-4-sulphate, chondroitin-6-sulphate, heparin and polystyrene sulphonate that were stable in sodium chloride solution of 0.1 M. The complexes of collagen with hyaluronic acid, or carboxymethylcellulose were less stable. The effect of pH variations (3.0–9.0) on the binding was investigated. Critical electrolyte concentrations (NaCl) were determined for complexes of collagen with glycosaminoglycans that dissociated at salt concentrations below that at which collagen precipitates. The values obtained were, 0.1 M for hyaluronic acid, and ∼0.5 M for chondroitin sulphate.
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