A novel carbonic anhydrase from the mantle of the pearl oyster (Pinctada fucata). Yu, Z., Xie, L., Lee, S., & Zhang, R. Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 143(2):190-4, 2, 2006.
A novel carbonic anhydrase from the mantle of the pearl oyster (Pinctada fucata). [pdf]Paper  A novel carbonic anhydrase from the mantle of the pearl oyster (Pinctada fucata). [link]Website  abstract   bibtex   
A novel carbonic anhydrase (CA) has been purified from the mantle of the pearl oyster, Pinctada fucata, by ammonium sulfate precipitation and affinity chromatography. Its molecular mass was determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) to be approximately 38 kDa. Native-PAGE shows that the novel CA can bind a fluorescent probe, 5-dimethylamino-1-naphthalenesulfonamide (DNSA), known to specifically bind carbonic anhydrase. Compared to carbonic anhydrase I (CAI) from human erythrocytes, the novel CA migrates faster indicating that it is more acidic. The effect of an inhibitor on the enzyme activity was also examined. The CA from the mantle showed a weak resistance to acetazolamide (AZ), a specific inhibitor of CA. When DNSA was bound to CA, it caused the wavelength of emission maximum intensity to blue shift to 454 nm upon excitation at 326 nm. Histochemical data indicates that the enzyme is distributed widely throughout the mantle tissue, being concentrated at the edge of the mantle. The evidence presented indicates a function for CA in the process of pearl formation and biomineralization.
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 title = {A novel carbonic anhydrase from the mantle of the pearl oyster (Pinctada fucata).},
 type = {article},
 year = {2006},
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 keywords = {Acetazolamide,Acetazolamide: pharmacology,Animals,Carbonic Anhydrases,Carbonic Anhydrases: analysis,Carbonic Anhydrases: chemistry,Carbonic Anhydrases: isolation & purification,Electrophoresis, Polyacrylamide Gel,Enzyme Inhibitors,Enzyme Inhibitors: pharmacology,Molecular Weight,Pinctada,Pinctada: enzymology,Tissue Distribution},
 pages = {190-4},
 volume = {143},
 websites = {http://www.ncbi.nlm.nih.gov/pubmed/16406278},
 month = {2},
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 abstract = {A novel carbonic anhydrase (CA) has been purified from the mantle of the pearl oyster, Pinctada fucata, by ammonium sulfate precipitation and affinity chromatography. Its molecular mass was determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) to be approximately 38 kDa. Native-PAGE shows that the novel CA can bind a fluorescent probe, 5-dimethylamino-1-naphthalenesulfonamide (DNSA), known to specifically bind carbonic anhydrase. Compared to carbonic anhydrase I (CAI) from human erythrocytes, the novel CA migrates faster indicating that it is more acidic. The effect of an inhibitor on the enzyme activity was also examined. The CA from the mantle showed a weak resistance to acetazolamide (AZ), a specific inhibitor of CA. When DNSA was bound to CA, it caused the wavelength of emission maximum intensity to blue shift to 454 nm upon excitation at 326 nm. Histochemical data indicates that the enzyme is distributed widely throughout the mantle tissue, being concentrated at the edge of the mantle. The evidence presented indicates a function for CA in the process of pearl formation and biomineralization.},
 bibtype = {article},
 author = {Yu, Zhenyan and Xie, Liping and Lee, Seunghwan and Zhang, Rongqing},
 journal = {Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology},
 number = {2}
}
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