Abstract
Fractionation of the highly purified but low active recombinant protein destabilase-lysozyme (Dest-Lys) by cation exchange chromatography on a TSK CM 3-SW chromatography the non-active fraction (IV) containing 90% of total protein has been separated. Fractions I, II, and III contained proteins with lysozyme and isopeptidase activities and their lysozyme activity correlated with the activity of native Dest-Lys. However, the ratio of lysozyme and isopeptidase activities differed in these fractions; maximal lysozyme activity was found in fraction III, while maximal isopeptidase activity was associated with fraction I. Possible regulation of different functions of Dest-Lys is discussed in the context of formation of its various complexes.
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Original Russian Text © Yu.I. Fadeeva, N.V. Antipova, I.P. Baskova, L.L. Zavalova, 2014, published in Biomeditsinskaya Khimiya.
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Fadeeva, Y.I., Antipova, N.V., Baskova, I.P. et al. Highly active fractions of the medicinal leech recombinant destabilase-lysozyme. Biochem. Moscow Suppl. Ser. B 8, 69–72 (2014). https://doi.org/10.1134/S199075081401003X
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DOI: https://doi.org/10.1134/S199075081401003X