Phospholipid catabolism enzymes of leptospires

Phospholipase A2, C, D activities of pathogenic (VGNCI-3, HS-26) and saprophytic (K-1028, G-80) strains of leptospires were determined. The strains used synthesized intracellular and extracellular forms of these esterases. To a considerable degree the endophospholipase activity was associated with the membrane structures. Differences in substrate specificity, Km, Vmax pH optimum values between exophospholipases of pathogenic and saprophytic leptospires used in the experiments are demonstrated. © 1992, Gustav Fischer Verlag, Stuttgart · New York. All rights reserved.

Авторы
Khisamov G.Z.1 , Morozova N.K.1
Редакторы
-
Издательство
-
Номер выпуска
3
Язык
Английский
Страницы
347-355
Статус
Опубликовано
Подразделение
-
Номер
-
Том
276
Год
1992
Организации
  • 1 Microbiology Laboratory, Medical Faculty, Patrice Lumumba Friendship University, Moscow, Russian Federation
Ключевые слова
phospholipase; phospholipid; article; chemistry; enzyme specificity; enzymology; Leptospira; Leptospira interrogans; metabolism; pH; thin layer chromatography; Chromatography, Thin Layer; Hydrogen-Ion Concentration; Leptospira; Leptospira Interrogans serovar canicola; Phospholipases; Phospholipids; Substrate Specificity
Дата создания
19.10.2018
Дата изменения
19.10.2018
Постоянная ссылка
https://repository.rudn.ru/ru/records/article/record/1056/