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Abstract

A new aminopeptidase was isolated from the biomass of the flagellate Astasia longa by precipitation with ammonium sulfate, gel filtration, and affinity chromatography on Arginine-Silochrome in 41% yield and with purification degree 490. The enzyme is irreversible inhibited by mercury chloride, EDTA, o-phenanthroline and, partially, bestatin and zinc chloride. It has an optimum pH 8.5 toward the hydrolysis of a synthetic chromogenic substrate Ala-pNA. The enzyme molecular mass is 45 kDa, isoelectric point 5.5, and temperature optimum 45°C. The enzyme most effectively hydrolyzes p-nitroanilides of alanine, arginine, and leucine; it is classified as metalloaminopeptidase.

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References

  1. Berthonneau, J., Rodier, M.N., Moudni, B., and Jacquemin, J.L., Exp. Parasitol., 2000, vol. 95, pp. 158–162.

    Article  PubMed  CAS  Google Scholar 

  2. Millership, J.J., Chappell, C., Okhuysen, P.C., and Snowden, K.F., J. Parasitol., 2002b, vol. 88, pp. 843–848.

    PubMed  CAS  Google Scholar 

  3. Waters, P.F., Snowden, K.F., and Holman, P.J., Parasitol. Res., 2004, vol. 93, pp. 410–418.

    Article  PubMed  Google Scholar 

  4. Bertin, P.B., Lozzi, S.P., Howel, J.K., Restrepo-Cadavid, G., Neves, D., Teixeira, A.R.L., de Sons, M.V., Norris, S.J., and Santana, J.M., Infection and Immunity, 2005, vol. 73, pp. 2253–2261.

    Article  PubMed  CAS  Google Scholar 

  5. Gardiner, D.L., Trenholm, K.R., Skinner-Adams, T.S., Stack, C.M., and Dalton, J.P., J. Biol. Chem., 2006, vol. 281, pp. 1741–1745.

    Article  PubMed  CAS  Google Scholar 

  6. Mucha, A., Kafarski, P., Lua, BellA., and Dalton, J.P., J. Biol. Chem., 2007, vol. 282, pp. 2069–2080.

    PubMed  Google Scholar 

  7. Buetow, D.E. and Padilla, G.M., J. Protozool., 1963, vol. 10, pp. 121–125.

    PubMed  CAS  Google Scholar 

  8. Erlanger, B.F., Kokovsky, N., and Cochen, W., Arch. Biochem. Biophys., 1961, vol. 95, pp. 271–278.

    Article  PubMed  CAS  Google Scholar 

  9. Chernyak, V.Ya. and Magretova, N.N., Anal. Biochem., 1982, vol. 123, pp. 101–109.

    Article  PubMed  CAS  Google Scholar 

  10. Fetterer, R.H., Miska, K.B., and Barfield, R.C., J. Parasitol., 2005, vol. 91, pp. 1280–1286.

    Article  PubMed  CAS  Google Scholar 

  11. Vander Jagt, D.L., Baack B.R., and Hunsaker L.A., Mol. Biochem. Parasitol., 1984, vol. 10, pp. 45–54.

    Article  Google Scholar 

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Correspondence to G. N. Rudenskaya.

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Original Russian Text © Yu.A. Rudenskaya, V.V. Aseev, G.N. Rudenskaya, 2008, published in Bioorganicheskaya Khimiya, 2008, Vol. 34, No. 3, pp. 333–336.

Abbreviations: All amino acids belong to L-series, if other is not stated.

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Rudenskaya, Y.A., Aseev, V.V. & Rudenskaya, G.N. Endocellular aminopeptidase from Astasia longa . Russ J Bioorg Chem 34, 300–303 (2008). https://doi.org/10.1134/S1068162008030084

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  • DOI: https://doi.org/10.1134/S1068162008030084

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