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Immunological Investigations
A Journal of Molecular and Cellular Immunology
Volume 15, 1986 - Issue 8
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Original Article

Binding Specificity of Mouse Serum Amyloid P-Component for Fibronectin

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Pages 749-761 | Published online: 07 Jul 2009
 

Abstract

Binding between purified mouse serum amyloid P-component (SAP) and plasma fibronectin (Fn) occurred when either one of the proteins was immobilized by specific antibody and the second protein was offered in a soluble form. Binding of Fn to immobilized SAP was cooperative and saturable at a molar ratio of SAP/Fn = 7.1. The molar ratio at saturation was 3.7 for SAP/Fn when SAP was allowed to bind to immobilized Fn. The binding required 2 to 3mM amounts of Ca++. The binding of SAP to Fn was selectively inhibited by a monoclonal antibody specific for the mid-molecule region of Fn, by soluble gelatin, and by heparin in the presence of 3mM Ca++. We conclude that the SAP binding site was localized at the mid-molecule region of Fn that includes the adjacent gelatin-binding domain and the heparin-I binding domain.

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