title: On self-organized shell formation by bovine carbonic anhydrase II, and soluble protein extracted from regenerated shell.
abstract: The soluble protein of hemocytes from diseased shell (HDS) of oyster, Crassostrea gigas, was shown to play a key role in the rapid growth of calcium carbonate crystals. In this study, we compared HDS extracted from regenerated (or diseased) shell with bovine carbonic anhydrase II in terms of their ability to promote the growth of calcium carbonate crystals. On the basis of scanning electron microscopy (SEM) and Fourier transform infrared (FT-IR) analysis, a high growth rate of calcium carbonate crystals was identified under artificial seawater and atmospheric temperature. The function and role of HDS extracted from regenerated shell are discussed at the molecular point as compared to aragonite-specific soluble proteins. Our findings suggest that hemocytes function as a soluble protein, with repeated GX (G: Gly, X: Asp, Asn or Glu) or negative charged amino acid domains binding calcium and specific surface features for catalyzing rapid shell regeneration.
authors.affiliation: Department of Chemical & Biomolecular Engineering, Korea Advanced Institute of Science and Technology, Gwahangno 335, Yuseonggu, Daejeon 305-701, Republic of Korea.
authors.forename: Seung Woo
authors.initials: SW
authors.lastname: Lee
authors.forename: Seung Bin
authors.initials: SB
authors.lastname: Park
authors.forename: Cheong Song
authors.initials: CS
authors.lastname: Choi
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002119:Calcium Carbonate / Q000737:chemistry*; D024402:Carbonic Anhydrase II / Q000502:physiology*; D002417:Cattle; D003460:Crystallization; D006434:Hemocytes / Q000502:physiology*; D008855:Microscopy, Electron, Scanning; D008969:Molecular Sequence Data; D010125:Ostreidae / Q000502:physiology*; D012038:Regeneration; D017550:Spectroscopy, Fourier Transform Infrared; D013499:Surface Properties
chemical_list: D024402:Carbonic Anhydrase II; D002119:Calcium Carbonate