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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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