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Novel salt-resistant alkaline phosphatase from eggs of the sea urchin Strongylocentrotus intermedius

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Abstract

It was shown that the alkaline phosphatase (AP) isolated from eggs of the sea urchin Strongylocentrotus intermedius was a homodimer with a molecular mass of 150 kDa and that it exhibited maximal activity at a рН of 8.1–8.5 and a temperature of 45°С. Mg2+, Ca2+, and Mn2+ ions, as well as DTT, are activators of AP activity, while Zn2+, Cu2+, Cd2+, Pb2+, and Ni2+ ions, as well as EDTA, N-EMI, and p-CMB, inhibit its activity. The enzyme demonstrates unique salt resistance and can hydrolyze the substrate in seawater. It was shown by fluorescence methods and circular dichroism that an increase of the NaCl concentration above 1.0М caused noticeable changes in the secondary and tertiary structures of the protein and a decrease in enzyme activity. Analysis of the molecular masses of tryptic peptides conducted by mass spectrometry with the MASCOT program (which is based on the NCBI and SWISS-PROT databases) did not allow identification of the investigated protein. The uniqueness of the source and of the properties of the investigated AP, which were not characteristic for nonspecific AP, as well as the difficulties in primary structure identification with the fingerprinting technique, suggested that this enzyme was a nontypical AP with a novel structure.

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References

  1. Coleman, J.E., Annu. Rev. Biophys. Biomol. Struct., 1992, vol. 21, no. 1, pp. 441–83.

    Article  CAS  PubMed  Google Scholar 

  2. Pfohl, R.J., Dev. Biol., 1975, vol. 44, no. 2, pp. 333–345.

    Article  CAS  PubMed  Google Scholar 

  3. Plisova, E.Yu., Balabanova, L.A., Ivanova, E.P., Kozhemyako, V.B., Mikhailov, V.V., Agafonova, E.V., and Rasskazov, V.A., Mar. Biotechnol., 2005, vol. 7, no. 3, pp. 173–178.

    Article  CAS  Google Scholar 

  4. Zueva, N.N., Dalaev, P.G., and Lazarova, D.L., Biokhimiya, 1993, vol. 58, no. 7, pp. 1009–1023.

    CAS  Google Scholar 

  5. Asgeirsson, B., Hartemink, R., and Chlebowski, J.F., Comp. Biochem. Physiol., 1995, vol. 110 B, no. 2, pp. 315–329.

    Article  Google Scholar 

  6. Nilsen, I.W., Overbo, K., and Olsen, R.L., Comp. Biochem. Physiol., 2001, vol. 129 B, no. 4, pp. 853–861.

    Article  CAS  Google Scholar 

  7. Wu, H.-T., Li, D.-M., Zhu, B.-W., Cheng, J.-H., Sun, J.-J., Wang, F.-L., Yang, Y., Song, Y.-K., and Yu, C.-X., Fisheries Sci., 2013, vol. 79, no. 3, pp. 477–485.

    Article  CAS  Google Scholar 

  8. Wende, A., Johansson, P., Ronnald, V., Dyall-Smith, M., Oesterhelt, D., and Grininger, M., J. Mol. Biol., 2010, vol. 400, no. 1, pp. 52–62.

    Article  CAS  PubMed  Google Scholar 

  9. Ishibashi, M., Yamashita, S., and Tokunaga, M., Biosci. Biotechnol. Biochem., 2005, vol. 69, no. 6, pp. 1213–1216.

    Article  CAS  PubMed  Google Scholar 

  10. Menzorova, N.I., Ivleva, A.D., Sibirtsev, Yu.T., and Rasskazov, V.A., Appl. Biochem. Microbiol., 2008, vol. 44, no. 1, pp. 106–110.

    Article  CAS  Google Scholar 

  11. Muginova, S.V., Zhavoronkova, A.M., and Shekhovtsova, T.N., Zh. Analit. Khim., 2005, vol. 60, no. 3, pp. 247–263.

    Google Scholar 

  12. Kas’yanov, V.L. Reproduktivnaya strategiya morskikh dvustvorchatykh mollyuskov i iglokozhikh (Reproductive Strategy of Marine Bivalves and Echinoderms), Leningrad: Nauka, 1989.

    Google Scholar 

  13. Durkina, V.B. and Evtushenko, Z.S., Mar. Ecol. Progr. Ser., 1991, vol. 72, nos. 1/2, pp. 111–115.

    Article  CAS  Google Scholar 

  14. Menzorova, N.I., Seitkalieva, A.V., and Rasskazov, V.A., Mar. Pollut. Bull., 2014, vol. 79, no. 1, pp. 188–195.

    Article  CAS  PubMed  Google Scholar 

  15. Seitkalieva, A.V., Menzorova, N.I., and Rasskazov, V.A., Russ. J. Mar. Biol., 2015, vol. 41, no. 1, pp. 51–59.

    Article  CAS  Google Scholar 

  16. Menzorova, N.I. and Rasskazov, V.A., Biokhimiya, 1980, vol. 45, no. 3, pp. 544–553.

    CAS  Google Scholar 

  17. Bredford, M., Anal. Biochem., 1976, vol. 72, nos. 1–2, pp. 248–254.

    Article  Google Scholar 

  18. Laemmli, U.K., Nature, 1970, vol. 227, pp. 680–685.

    Article  CAS  PubMed  Google Scholar 

  19. Chen, P.S., Toribar, N., Ir, T.Y., and Warne, H., Anal. Chem., 1956, vol. 28, no. 11, pp. 1756–1758.

    Article  CAS  Google Scholar 

  20. Sreerama, N. and Woody, R.W., Anal. Biochem., 2000, vol. 287, no. 2, pp. 252–60.

    Article  CAS  PubMed  Google Scholar 

  21. Olsen, R.L., Overbo, K., and Myrnes, B., Comp. Biochem. Physiol., 1991, vol. 99B, no. 4, pp. 755–761.

    Google Scholar 

  22. Chuang, N.-N., Comp. Biochem. Physiol., 1990, vol. 95B, no. 1, pp. 165–169.

    CAS  Google Scholar 

  23. Homaei, A., J. Mol. Catalysis B: Enzymatic, 2015, vol. 118, pp. 16–22.

    Article  CAS  Google Scholar 

  24. Xiao, R., Xie, L.-P., Lin, J.-Y., Li, C.-H., Chen, Q.-X., Zhou, H.-M., and Zang, R.-Q., J. Mol. Catalysis, 2002, vol. 17B, no. 2, pp. 65–74.

    Article  CAS  Google Scholar 

  25. Liao, J.H., Chen, Q.X., Zhang, Q., Yang, Y., and Shi, Y., Appl. Biochem. Biotechnol., 2009, vol. 158, no. 2, pp. 323–333.

    Article  CAS  PubMed  Google Scholar 

  26. Hauksson, J.B., Andresson, O.S.;., and Asgeirsson, B., Enzyme Microb. Technol., 2000, vol. 27, no. 1, pp. 66–73.

    Article  CAS  PubMed  Google Scholar 

  27. Pinoni, S.A., Goldemberg, A.L., and Lopez-Mananes, A.A., J. Exp. Mar. Biol. Ecol., 2005, vol. 326, no. 2, pp. 217–226.

    Article  CAS  Google Scholar 

  28. Lee, A.-C. and Chuang, N.-N., Comp. Biochem. Physiol., 1991, vol. 99, no. 4, pp. 845–850.

    Google Scholar 

  29. Zhang, R.-Q., Chen, Q.-X., Xiao, R., Xie, L.-P., Zeng, X.-G., and Zhou, H.-M., Biochim. Biophys. Acta, 2001, vol. 1545, no. 1, pp. 6–12.

    Article  CAS  PubMed  Google Scholar 

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Authors and Affiliations

  1. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, Vladivostok, 690022, Russia

    A. V. Seitkalieva, N. I. Menzorova, T. I. Vakorina, P. S. Dmitrenok & V. A. Rasskazov

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  1. A. V. Seitkalieva
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  2. N. I. Menzorova
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  3. T. I. Vakorina
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  4. P. S. Dmitrenok
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  5. V. A. Rasskazov
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Correspondence to A. V. Seitkalieva.

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Original Russian Text © A.V. Seitkalieva, N.I. Menzorova, T.I. Vakorina, P.S. Dmitrenok, V.A. Rasskazov, 2017, published in Prikladnaya Biokhimiya i Mikrobiologiya, 2017, Vol. 53, No. 1, pp. 16–25.

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Seitkalieva, A.V., Menzorova, N.I., Vakorina, T.I. et al. Novel salt-resistant alkaline phosphatase from eggs of the sea urchin Strongylocentrotus intermedius . Appl Biochem Microbiol 53, 11–19 (2017). https://doi.org/10.1134/S0003683817010173

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  • DOI: https://doi.org/10.1134/S0003683817010173

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