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.
Khisamov
G Z
GZ
Microbiology Laboratory, Medical Faculty, Patrice Lumumba Friendship University, Moscow, Russia.
Morozova
N K
NK
D002855:Chromatography, Thin Layer; D006863:Hydrogen-Ion Concentration; D007919:Leptospira / Q000201:enzymology*; D041341:Leptospira interrogans serovar canicola / Q000201:enzymology*; D010740:Phospholipases / Q000737:chemistry / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism*; D013379:Substrate Specificity
D010743:Phospholipids; D010740:Phospholipases