Phospholipase activity of Helicobacter pylori and its inhibition by bismuth salts. Biochemical and biophysical studies.

@article{Ottlecz1993PhospholipaseAO,
  title={Phospholipase activity of Helicobacter pylori and its inhibition by bismuth salts. Biochemical and biophysical studies.},
  author={Anna Ottlecz and Jim J. Romero and Stuart L. Hazell and David Y Graham and Lenard M. Lichtenberger},
  journal={Digestive diseases and sciences},
  year={1993},
  volume={38 11},
  pages={2071-80}
}
In this study we measured phospholipase A (PLA) and C (PLC) activity of media filtrates and French Press lysates of the gastritis-inducing bacteria Helicobacter pylori. We report here that both H. pylori lysates and filtrates contain PLA1, PLA2, and C enzymes, which readily hydrolyze a radiolabeled dipalmitoylphosphatidylcholine (DPPC) and phosphorylcholine substrates, respectively. The specific activity of both PLA and C enzymes were greatest in the 6.5-7.0 and 8.4-8.8 pH ranges, respectively… CONTINUE READING
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