Location and analysis of byssal structural proteins of Mytilus edulis.
The acellular attachment organ (byssus) of the marine mussel Mytilus edulis L. is composed of threads that emanate from the body of the mussel to adhesive discs that anchor the threads to rocks, sand and other mussels. Three proteins have been purified by immunohistological methods and located to specific regions of the byssus. A collagenous protein with subunit molecular weights of 53,000, 55,000 and 65,000 is found in the matrix of the elastic thread region. Its 73,000-MW precursor was extracted from foot glands in the area proximal to the animal body and was identified by immune cross-reactivity. A cystine-rich, acidic protein was found in all regions of the byssus associated with a third protein, the polyphenolic protein. The L-dopa-containing polyphenolic protein appears in the cortex of the entire thread and adhesive plaque and at the substrate-plaque interface. Antiserum to this protein stains spherical vesicles in the phenol gland of the foot. Using immuno-electrophoretic methods, the polyphenolic protein and the cystine-rich protein were shown to form high molecular weight aggregates with aging of the byssus.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D049872:Bivalvia / Q000032:analysis* / Q000166:cytology; D003094:Collagen / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D003012:Microbial Collagenase; D008970:Molecular Weight; D011506:Proteins / Q000032:analysis*
D000596:Amino Acids; D046911:Macromolecular Substances; D011506:Proteins; D003094:Collagen; D003012:Microbial Collagenase