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Interactions between chondroitin sulfate and concanavalin A.
Biochimica Et Biophysica Acta
|February 1, 1978
Summary
Concanavalin A binds to chondroitin sulfate and other glycosaminoglycans, forming insoluble complexes at low pH and low salt concentrations. These interactions are reversible and depend on electrostatic forces, not occurring under physiological conditions.
Area of Science:
- Biochemistry
- Glycobiology
- Molecular Interactions
Background:
- Chondroitin sulfate is a major component of the extracellular matrix.
- Concanavalin A is a lectin known to bind carbohydrates.
Purpose of the Study:
- To investigate the binding interactions between concanavalin A and chondroitin sulfate.
- To determine the conditions under which these interactions occur and their nature.
Main Methods:
- Precipitin reactions at varying pH and ionic strength.
- Affinity chromatography using Sephadex G-200.
- Fractionation using Bio-Gel P-200.
Main Results:
- Insoluble complexes formed between concanavalin A and chondroitin sulfate below pH 5.4.
- Interactions were concentration-dependent and optimal within specific ranges.
- Similar interactions observed with hyaluronic acid and heparin.
- No significant precipitation occurred in physiological salt solutions at neutral pH.
- Chondroitin sulfate promoted concanavalin A self-aggregation at pH 7.3, but no stable complexes formed.
Conclusions:
- Binding is primarily mediated by reversible, non-specific electrostatic interactions.
- Low pH and low ionic strength are crucial for complex formation.
- Interactions are not stable under physiological conditions (neutral pH, physiological salt concentrations).