| Literature DB >> 17779975 |
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.Entities:
Year: 1981 PMID: 17779975 DOI: 10.1126/science.212.4498.1038
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728