Heparin and Concanavalin A interaction as a model for studying the mechanism of the anticoagulant activity
A systematic study of the role of the Ca2+ and Mn2+ ions on the interaction between heparin and Concanavalin A was carried out. The protein was demetallized, and complex formation was followed by a light scattering assay. In the absence of ions no visible interaction was detected. Maximum activity w...
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1989
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00493848_v54_n3_p237_Monge http://hdl.handle.net/20.500.12110/paper_00493848_v54_n3_p237_Monge |
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| Sumario: | A systematic study of the role of the Ca2+ and Mn2+ ions on the interaction between heparin and Concanavalin A was carried out. The protein was demetallized, and complex formation was followed by a light scattering assay. In the absence of ions no visible interaction was detected. Maximum activity was obtained when Mn2+ ions were added. A similar effect was observed when Ca2+ ions alone were used. Kinetics of the interaction in the presence of optimal Mn2+ and (or) Ca2+ concentrations confirmed the role of Ca2+ in accelerating a conformational change leading to a functional protein. A peculiar effect of activation-inhibition depending on ion concentration was also exhibited by Ca2+. These results confirm that Ca2+ and Mn2+ can occupy both sites on Concanavalin A and activate the protein for binding heparin. They point also to a crucial role of Ca2+ in the binding capacity of the active heparin fraction. |
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