[Purification and properties of recombinant Erwinia carotovora L-asparaginase expressed in E.coli cells]

Авторы: Borisova A.A., El’darov M.A., Zhgun A.A., Aleksandrova S.S., Omel’ianiuk N.M., Sokov B.N., Berezov T.T., Sokolov N.N.
Журнал: Biomeditsinskaia khimiia
Том: 49
Номер: 5
Год издания: 2003
Издательство: Rossiiskaya Akademiya Meditsinskikh Nauk
Местоположение издательства: Russian Federation
Первая страница: 502
Последняя страница: 507
Аннотация: The method of purification Erwinia carotovora recombinant L-asparaginase, expressed in E.coli, including ultrasonic disintegration of biomass, fractionation ammonium sulfate and column chromatography on CM- or SP-Sepharose has been developed. According to SDS-PAAGE the enzyme preparation was homogeneous, its specific activity and yield consist respectively about 620 IU/mg of protein and 75%. Physical-chemical and structural properties of recombinant Erwinia carotovora L-asparaginase are similar to the enzymes from the wild strains Erwinia carotovora and recombinant L-asparaginase Erwinia chrysanthemi.
Добавил в систему: Эльдаров Михаил Анатольевич

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