Abstract
The urease activity of Campylobacter pylori was measured over a range of pH values. In a citrate-Hepes system, two peaks of activity were seen, at pH 5 and at pH 8. The former activity was inhibited by phosphate. Gastric campylobacter-like organisms isolated from the stomachs of several mammals resembled C. pylori in possessing two urease activities with different pH optima.
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