Highly active fractions of the medicinal leech recombinant destabilase-lysozyme |
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| Authors: | Yu. I. Fadeeva N. V. Antipova I. P. Baskova L. L. Zavalova |
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| Affiliation: | 1. Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117997, Russia
2. Biological Faculty, Lomonosov Moscow State University, Moscow, 119991, Russia
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| 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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