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Catalytic sites of medicinal leech enzyme destabilase-lysozyme (Mldl). Structure-functional correlationстатья
Информация о цитировании статьи получена из
Scopus
Дата последнего поиска статьи во внешних источниках: 19 сентября 2015 г.
- Авторы: Zavalova LL, Antipova NV, Fadeeva IuI, Pavliukov MS, Pletneva NV, Pletnev VZ, Baskova IP
- Журнал: Bioorganicheskaia khimiia
- Том: 38
- Номер: 2
- Год издания: 2012
- Первая страница: 229
- Последняя страница: 233
- DOI: 10.1134/S1068162012020148
- Аннотация: 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.
- Добавил в систему: Фадеева Юлия Игоревна