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STABILITY OF COLLAGENOLYTIC PROTEASE ISOZYME-C FROM THE CRAB PARALITHODES CAMTSCHATICAстатья
Информация о цитировании статьи получена из
Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 29 мая 2015 г.
- Авторы: SAKHAROV IY, LITVIN FE
- Журнал: Biochemistry (Moscow)
- Том: 59
- Номер: 2
- Год издания: 1994
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 175
- Последняя страница: 177
- Аннотация: The stability of isozyme C of the collagenolytic protease from the crab Paralithodes camtschatica has been determined. The protease was shown to be stable under mildly alkaline conditions. Under these conditions significant decrease in enzyme activity was observed only at temperature above 40 degrees C; the thermal inactivation of the protease is monomolecular. Neither CaCl2 nor NaCl influence the thermal stability of protease C. At pH < 6.0 rapid irreversible inactivation of protease C was found, probably due to autolysis. Under acidic conditions the presence of CaCl2 significantly stabilized the enzyme, this effect showing an extremum with the concentration of the salt. Increasing the enzyme concentration also greatly stabilized protease C. Protease C is labile under highly alkaline conditions. Inactivation of protease C at pH 11.25 is concentration independent. The activity of the protease is stable to detergents, but it is effectively inactivated by guanidine-HCl.
- Добавил в систему: Сахаров Иван Юрьевич