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Biofouling
The Journal of Bioadhesion and Biofilm Research
Volume 14, 1999 - Issue 3
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Original Articles

Purification and characterization of a dopa‐containing protein from the foot of the Asian freshwater mussel, Limnoperna fortunei

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Pages 181-188 | Received 15 Mar 1999, Accepted 25 Jun 1999, Published online: 09 Jan 2009
 

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.

Notes

Corresponding author; fax: 81–268–21–5571; e‐mail: [email protected]‐u.ac.jp

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