Highly active fractions of the medicinal leech recombinant destabilase-lysozyme


1. Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences
2. Biological Faculty, Lomonosov Moscow State University
Type: Experimental study
DOI: 10.18097/pbmc20146003332      UDK: 577.112.083      PubMed Id: 25019395
Year: 2014 vol: 60  issue:3  pages: 332-337
Abstract: From the highly purified but lowly active recombinant protein Destabilas-Lysozyme (Dest-Lys) by use cation-exchange column TSK CM 3-SW chromatography, it was separated non-active fraction IV, contained 90% of protein. Fractions I, II and III, represented proteins with lysozyme and isopeptidase activities. Their lysozyme activity correlates with the activity of natural Des-Lys. The ratio of the activities in fractions I – III is such, that maximal lysozyme activity is concentrated in fraction III, isopeptidase – in fraction I. It is discussed the possibility of Dest-Lys different functions regulation is depended on the formation of protein complex forms
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Reference: Fadeeva Yu.I., Antipova N.V., Baskova I.P., Zavalova L.L., Highly active fractions of the medicinal leech recombinant destabilase-lysozyme, Biomeditsinskaya khimiya, 2014, vol: 60(3), 332-337.
This paper is also available as the English translation:10.1134/S199075081401003X
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