Abstract
A gelatin-binding protein of 215 kDa subunit molecular weight was isolated from the hemolymph of Mytilus galloprovincialis. Using Western blotting analysis the protein reacted with polyclonal antiserum but not with monoclonal antibody against human plasma fibronectin. The rabbit antiserum prepared utilizing the isolated protein from Mytilus as the immunogen strongly reacted with the same gelatin-binding protein and also with human, bovine and chicken plasma fibronectin. The antiserum is suitable for cytochemical localization of fibronectin-like molecule in mussel tissues using either immunoperoxidase or immunogold staining. The data reported here indicate that the gelatin-binding protein purified from Mytilus displays molecular and immunological properties similar to those of vertebrate fibronectin.
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