Highly active fractions of the medicinal leech recombinant destabilase-lysozyme

   
Fadeeva Yu.I.1 , Antipova N.V.1, Baskova I.P.2, Zavalova L.L.1

1. Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences
2. Biological Faculty, Lomonosov Moscow State University
Section: Experimental Study
DOI: 10.18097/PBMC20146003332      PubMed Id: 25019395
Year: 2014  Volume: 60  Issue: 3  Pages: 332-337
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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Keywords: destabilase-lysozyme of Hirudo medicinalis, lysozyme and isopeptidase functions, forms of recombinant enzyme
Citation:

Fadeeva, Yu. I., Antipova, N. V., Baskova, I. P., Zavalova, L. L. (2014). Highly active fractions of the medicinal leech recombinant destabilase-lysozyme. Biomeditsinskaya Khimiya, 60(3), 332-337.
This paper is also available as the English translation: 10.1134/S199075081401003X
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