A Dopa‐containing protein was purified from the foot of the Asian freshwater mussel, Limnoperna fortunei, through acid‐urea extraction, 36% ammonium sulfate precipitation, Sephacryl S‐200 gel filtration, and reversed phase high performance liquid chromatogra‐phy. The apparent molecular mass of the protein was 96 kDa, and Achromobacter protease I digested this into six major fragments. The amino acid sequences of the fragments were determined as two hexapeptides and four decapeptides. The consensus sequence of the decapeptides was Lys‐(Hyp/Pro)‐Thr‐(Gln/Tyr)‐Dopa‐(Ser/Thr)‐(Asp/Thr)‐Glu‐Tyr‐Lys. These results suggest that the Dopa‐containing foot protein mostly consists of repetitive decapeptides and hexapeptides. The Dopa‐containing 96 kDa protein is considered to be a byssal precursor in L. fortunei.
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