title: Purification and characterization of perlucin and perlustrin, two new proteins from the shell of the mollusc Haliotis laevigata.
abstract: Two new proteins, named perlucin and perlustrin, with M(r) 17,000 and 13,000, respectively, were isolated from the shell of the mollusc Halotis laevigata (abalone) by ion-exchange chromatography and reversed-phase HPLC after demineralization of the shell in 10% acetic acid. The sequence of the first 32 amino acids of perlucin indicated that this protein belonged to a heterogeneous group of proteins consisting of a single C-type lectin domain. Perlucin increased the precipitation of CaCO(3) from a saturated solution, indicating that it may promote the nucleation and/or the growth of CaCO(3) crystals. With pancreatic stone protein (lithostathine) and the eggshell protein ovocleidin 17, this is the third C-type lectin domain protein isolated from CaCO(3) biominerals. This indicates that this type of protein performs an important but at present unrecognized function in biomineralization. Perlustrin was a minor component of the protein mixture and the sequence of the first 33 amino acids indicated a certain similarity to part of the much larger nacre protein lustrin A.
authors.affiliation: Physik Department der TU-München, Institut für Biophysik, E22, James-Franck-Strasse, Garching, 85747, Germany.
authors.forename: I M
authors.initials: IM
authors.lastname: Weiss
authors.forename: S
authors.initials: S
authors.lastname: Kaufmann
authors.forename: K
authors.initials: K
authors.lastname: Mann
authors.forename: M
authors.initials: M
authors.lastname: Fritz
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002119:Calcium Carbonate; D002135:Calcium-Binding Proteins / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D016326:Extracellular Matrix Proteins / Q000737:chemistry* / Q000302:isolation & purification; D037102:Lectins / Q000737:chemistry* / Q000302:isolation & purification; D051847:Lithostathine; D008969:Molecular Sequence Data; D008974:Mollusca / Q000737:chemistry* / Q000166:cytology / Q000648:ultrastructure; D009419:Nerve Tissue Proteins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D002135:Calcium-Binding Proteins; D016326:Extracellular Matrix Proteins; D037102:Lectins; D051847:Lithostathine; D009419:Nerve Tissue Proteins; C403488:perlucin, Haliotis laevigata; C403490:perlustrin; D002119:Calcium Carbonate