Zoeken
Zoeken kan via de modus 'eenvoudig zoeken' (één veld) of uitgebreid via 'geavanceerd zoeken' (meerdere velden). Zo kan je bv. zoeken op een combinatie van een auteursnaam (auteur), een jaartal (jaar) en een documenttype.
Boekenmand
Nuttige resultaten kan je aanvinken en toevoegen aan een mandje. De inhoud hiervan kan je exporteren of afdrukken (naar bv. PDF).
RSS
Op de hoogte blijven van nieuw toegevoegde publicaties binnen uw interessegebied? Dit kan door een RSS-feed (?) te maken van jouw zoekopdracht.
nieuwe zoekopdracht
First insights into the biochemistry of tube foot adhesive from the sea urchin Paracentrotus lividus (Echinoidea, Echinodermata)
Santos, R.; da Costa, G.; Franco, C.; Gomes-Alves, P.; Flammang, P.; Coelho, A.V. (2009). First insights into the biochemistry of tube foot adhesive from the sea urchin Paracentrotus lividus (Echinoidea, Echinodermata). Mar. Biotechnol. 11(6): 686-698. dx.doi.org/10.1007/s10126-009-9182-5
In: Marine Biotechnology. Springer-Verlag: New York. ISSN 1436-2228; e-ISSN 1436-2236
|  |
| Trefwoorden |
Paracentrotus lividus (Lamarck, 1816) [WoRMS]
Marien/Kust |
| Author keywords |
Marine adhesion; Sea urchin; Tube feet footprints; Protein-based |
| Auteurs | | Top |
- Santos, R.
- da Costa, G.
- Franco, C.
|
- Gomes-Alves, P.
- Flammang, P.
- Coelho, A.V.
|
|
| Abstract |
Sea urchins are common inhabitants of wave-swept shores. To withstand the action of waves, they rely on highly specialized independent adhesive organs, the adoral tube feet. The latter are extremely well-designed for temporary adhesion being composed by two functional subunits: (1) an apical disc that produces an adhesive secretion to fasten the sea urchin to the substratum, as well as a deadhesive secretion to allow the animal to move and (2) a stem that bears the tensions placed on the animal by hydrodynamism. Despite their technological potential for the development of new biomimetic underwater adhesives, very little is known about the biochemical composition of sea urchin adhesives. A characterization of sea urchin adhesives is presented using footprints. The latter contain inorganic residues (45.5%), proteins (6.4%), neutral sugars (1.2%), and lipids (2.5%). Moreover, the amino acid composition of the soluble protein fraction revealed a bias toward six amino acids: glycine, alanine, valine, serine, threonine, and asparagine/aspartic acid, which comprise 56.8% of the total residues. In addition, it also presents higher levels of proline (6.8%) and half-cystine (2.6%) than average eukaryotic proteins. Footprint insolubility was partially overcome using strong denaturing and reducing buffers, enabling the visualization of 13 proteins by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The conjugation of mass spectrometry with homology-database search allowed the identification of six proteins: alpha and beta tubulin, actin, and histones H2B, H3, H2A, and H4, whose location and function in the adhesive are discussed but require further investigation. For the remaining unidentified proteins, five de novo-generated peptide sequences were found that were not present in the available protein databases, suggesting that they might be novel or modified proteins. |
IMIS is ontwikkeld en wordt gehost door het VLIZ.
