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.

Authors
Khisamov G.Z.1 , Morozova N.K.1
Number of issue
3
Language
English
Pages
347-355
Status
Published
Volume
276
Year
1992
Organizations
  • 1 Microbiology Laboratory, Medical Faculty, Patrice Lumumba Friendship University, Moscow, Russian Federation
Keywords
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
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