Abstract
The fouling marine mussel Mytilus edulis attaches itself to various substrates by spinning byssal threads, the adhesive discs of which are rich in the amino acid 3,4-dihydroxyphenylalanine (dopa). An acid-soluble protein was extracted and purified from the phenol gland located in the byssus-secreting foot of the animal. This protein is highly basic and contains large amounts of lysine, dopa, and 3- and 4-hydroxyproline. The composition of this protein and its sticky tendencies in vitro strongly suggest that it contributes to byssal adhesion.
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Publication Info
- Year
- 1981
- Type
- article
- Volume
- 212
- Issue
- 4498
- Pages
- 1038-1040
- Citations
- 1027
- Access
- Closed
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Identifiers
- DOI
- 10.1126/science.212.4498.1038