FIBRONECTIN FROM THE HEMOLYMPH OF THE MARINE BIVALVE MYTILUS-GALLOPROVINCIALIS - PURIFICATION, IMMUNOLOGICAL CHARACTERIZATION AND IMMUNOCYTOCHEMICAL LOCALIZATION

A gelatin-binding protein of 215 kDa subunit molecular weight was isol ated from the hemolymph of Mytilus gallopuovincialis. Using Western bl otting 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 a lso with human, bovine and chicken plasma fibronectin. The antiserum i s 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 pur ified from Mytilus displays molecular and immunological properties sim ilar to those of vertebrate fibronectin.