Calcite‐specific coupling protein in barnacle underwater cement

• DOI: 10.1111/j.1742-4658.2007.06161.x
• Publication Date: 2007-11-17T11:43:24Z
• Authors: Youichi Mori; Youhei Urushida; Masahiro Nakano; Susumu Uchiyama; Kei Kamino
• Keywords: 0301 basic medicine; Sequence Homology, Amino Acid; Circular Dichroism; Molecular Sequence Data; Thoracica; Proteins; Recombinant Proteins; Calcium Carbonate; Molecular Weight; 03 medical and health sciences; Adhesives; Animals; Electrophoresis, Polyacrylamide Gel; Adsorption; Amino Acid Sequence

The barnacle relies for its attachment to underwater foreign substrata on the formation of a multiprotein complex called cement. 20 kDa cement protein is component Megabalanus rosa cement, although specific function in has not, until now, been known. recombinant form expressed bacteria was purified soluble under physiological conditions, and confirmed retain almost same structure as that native protein. Both from adhesive layer were characterized. This revealed abundant Cys residues, which accounted 17% total intramolecular disulfide form, essential proper folding monomeric structure. adsorbed calcite metal oxides seawater, but not glass synthetic polymers. adsorption isotherm fitted Langmuir model well, indicating calcite‐specific adsorbent. An evaluation distribution molecular size solution by analytical ultracentrifugation indicated exists monomer 100 m 1 NaCl solution; thus, acts when interacting with surface. cDNA encoding homologous isolated Balanus albicostatus , derived amino acid sequence compared M. . Calcite major constituent both shell base periphery, also possible target due gregarious nature organisms. specificity may be related fact most frequent material attached