Purification and Characterization of Perlucin and Perlustrin, Two New Proteins from the Shell of the Mollusc Haliotis laevigata Export

@article{citeulike:2756438, abstract = {Two new proteins, named perlucin and perlustrin, with Mr 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 CaCO3 from a saturated solution, indicating that it may promote the nucleation and/or the growth of CaCO3 crystals. With pancreatic stone protein (lithostathine) and the eggshell protein ovocleidin 17, this is the third C-type lectin domain protein isolated from CaCO3 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.}, author = {Weiss, Ingrid M. and Kaufmann, Stefan and Mann, Karlheinz and Fritz, Monika}, citeulike-article-id = {2756438}, citeulike-linkout-0 = {http://dx.doi.org/10.1006/bbrc.1999.1907}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6WBK-45K1BR0-15F/1/e272cdedb1bf754f68e146d00587752c}, day = {7}, doi = {10.1006/bbrc.1999.1907}, journal = {Biochemical and Biophysical Research Communications}, keywords = {perlucin}, month = {January}, number = {1}, pages = {17--21}, posted-at = {2008-05-05 12:39:34}, priority = {5}, title = {Purification and Characterization of Perlucin and Perlustrin, Two New Proteins from the Shell of the Mollusc Haliotis laevigata}, url = {http://dx.doi.org/10.1006/bbrc.1999.1907}, volume = {267}, year = {2000} }

TY - JOUR ID - citeulike:2756438 L3 - citeulike-article-id:2756438 N2 - Two new proteins, named perlucin and perlustrin, with Mr 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 CaCO3 from a saturated solution, indicating that it may promote the nucleation and/or the growth of CaCO3 crystals. With pancreatic stone protein (lithostathine) and the eggshell protein ovocleidin 17, this is the third C-type lectin domain protein isolated from CaCO3 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. IS - 1 JF - Biochemical and Biophysical Research Communications EP - 21 TI - Purification and Characterization of Perlucin and Perlustrin, Two New Proteins from the Shell of the Mollusc Haliotis laevigata VL - 267 SP - 17 KW - perlucin AU - Weiss, Ingrid AU - Kaufmann, Stefan AU - Mann, Karlheinz AU - Fritz, Monika PY - 2000/01/07/ UR - http://dx.doi.org/10.1006/bbrc.1999.1907 ER -