Mussel adhesives molecular weight

Best understood of the invertebrate adhesive-mediated attachment mechanisms is that of the common blue mussel, Myiilus edulis, and its close relative, Mytilus californianus L. The mechanism includes the byssus, an acellular proteinaceous organ produced by glands inside the mussel, combined with a delivery system that secretes the byssus efficiently underwater. The protein that is the functional unit of the adhesive mixture was first purified from the gland where it originates and characterized by Waite and Tanzer (i). Called mussel adhesive protein (MAP), it is a high molecular weight (120,000 10,000 MW) basic protein,... 

Structural proteins such as collagen, elastin, and spider silk contain repeating sequences of amino acids. In 1983, Waite discovered that the protein secreted by the phenol gland of the blue sea mussel Mytilus edulis consists of closely related decapeptide and hexapeptide sequences with a combined molecular weight of approximately 130 kilodaltons (kDa).i He further elucidated that this protein is transformed into glue through enzymatic oxidation to form the adhesive plaques that anchor the mussel... 

The transformation of the mussel adhesive protein to glue involves a sequence of chemical events in which timing is a critical element. The redox enzyme (catechol oxidase) plays an important role. Recently, Waite has observed that the catechol oxidase is present at very high concentrations in ribbed mussels. At these concentration levels, it acts more like a reagent than a catalyst. Waite has also established that the enzyme shows an apparent molecular weight of 38 kDa and does not contain any metal atoms. Presumably it possesses a quinone cofactor at levels as high as one quinone/mg of enzyme. 

---