Gelatin-binding Immunoglobulins in Normal Bovine Serum

概要

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We found the 150-kDa and 900-kDa proteins in the gelatin-binding fraction during fibronectin purification from normal bovine serum. These proteins were separated from fibronectin by heparin column chromatography as the unbound fraction. The results of partial amino acid sequencing and the reactivity for anti-IgG antibody indicated that these proteins were immunoglobulin G and M, respectively, and both proteins had binding affinity to denatured collagen. We called these proteins Gelatin-Binding Immunoglobulins(GBIgs). GBIgs bound to gelatin much more strongly than to collagen. A whole IgG fraction which was purified from serum using protein G bound neither denatured collagen nor native collagen. GBIgs stimulated the adhesion of macrophage-like cells from bovine blood to denatured collagen that was not a good substrate for macrophage adhesion. On the other hand, GBIgs did not facilitate the adhesion of macrophage-like cells to native collagen. This result suggests that GBIgs can be the"bio-probe"for distinguishing native collagen from denatured collagen in the circulation system.
日本結合組織学会の論文
1999-09-25