DOI QR코드

DOI QR Code

Comparison of hemocytic carbonic anhydrase activity of bivalves

  • Cho, Sang-Man (School of Marine Applied Biosciences, Kunsan National University) ;
  • Jeong, Woo-Geon (Department of Seafood and Aquaculture Science, Gyeongsang National University) ;
  • Choi, Young-Joon (Department of Seafood and Aquaculture Science, Gyeongsang National University)
  • Received : 2016.03.11
  • Accepted : 2016.03.31
  • Published : 2016.03.31

Abstract

Carbonic anhydrase (CA), which is involved in shell formation processes in bivalves, is one of the major biocatalysts for carbon capture and storage. In this study we investigated CA activity in the total hemocytic proteins of five bivalves. The highest CA activity was observed in Scapharca broughtonii, which had more than twice the activity found in Crassostrea gigas. No CA activity was observed among the total hemocytic proteins of Pinctada fucata and Saxidomus purpuratus. The results suggest that marine invertebrates may provide a better source of CA, as an alternative to mammalian sources.

Keywords

References

  1. Gibbins, J. and Chalmers, H. (2008) Carbon capture and storage. Energy Policy, 36(12): 4317-4322. https://doi.org/10.1016/j.enpol.2008.09.058
  2. Henry, R.P. (1996) Multiple roles of carbonic anhydrase in cellular transport and metabolism. Annu Rev Physiol, 58: 523-538. https://doi.org/10.1146/annurev.ph.58.030196.002515
  3. Henry, R.P. and Saintsing, D.G. (1983) Carbonic Anhydrase Activity and Ion Regulation in Three Species of Osmoregulating Bivalve Molluscs. Physiological Zoology, 56(2): 274-280. https://doi.org/10.1086/physzool.56.2.30156059
  4. Lacis, A.A., Schmidt, G.A., Rind, D. and Ruedy, R.A. (2010) Atmospheric $CO_2$: Principal Control Knob Governing Earth's Temperature. Science, 330: 356-359. https://doi.org/10.1126/science.1190653
  5. Lee, S.-W., Park, S.-B., Jeong, S.-K., Lim, K.-S., Lee, S.-H. and Trachtenberg, M.C. (2010) On carbon dioxide storage based on biomineralization strategies. Micron, 41(4): 273-282. https://doi.org/10.1016/j.micron.2009.11.012
  6. Meldrum, N.U. and Roughton, F.J.W. (1933) Carbonic anhydrase. Its preparation and properties. The Journal of Physiology, 80(2): 113-142. https://doi.org/10.1113/jphysiol.1933.sp003077
  7. Miyamoto, H., Miyashita, T., Okushima, M., Nakano, S., Morita, T. and Matsushiro, A. (1996) A carbonic anhydrase from the nacreous layer in oyster pearls. Proceedings of the National Academy of Sciences, 93(18): 9657-9660. https://doi.org/10.1073/pnas.93.18.9657
  8. Miyashita, T., Takami, A. and Takagi, R. (2012) Molecular Cloning and Characterization of the 5′-Flanking Regulatory Region of the Carbonic Anhydrase Nacrein Gene of the Pearl Oyster Pinctada fucata and Its Expression. Biochemical Genetics, 50(9-10): 673-683. https://doi.org/10.1007/s10528-012-9510-8
  9. Norizuki, M. and Samata, T. (2008) Distribution and function of the nacrein-related proteins inferred from structural analysis. Mar Biotechnol., 10(3): 234-241. https://doi.org/10.1007/s10126-007-9061-x
  10. Wilbur, K.M. and Anderson, N.G. (1948) ELECTROMETRIC AND COLORIMETRIC DETERMINATION OF CARBONIC ANHYDRASE. Journal of Biological Chemistry, 176: 147-154.
  11. Yu, Z., Xie, L., Lee, S. and Zhang, R. (2006) A novel carbonic anhydrase from the mantle of the pearl oyster (Pinctada fucata). Comp. Biochem. Physiol. B. Biochem. Mol. Biol., 143(2): 190-194. https://doi.org/10.1016/j.cbpb.2005.11.006