Characterisation of the urease from Helicobacter pylori and comparison with the ureases from related spiral gastric bacteria.

ABSTRACT

The urease enzyme of Helicobacter pylori was partially purified from whole cell extracts and found to have a molecular weight of 484 +/- 12 kDa. Ten monoclonal antibodies (mAbs) were produced against four different epitopes of the native enzyme. These mAbs also recognised the ureases of H. pylori-like organisms isolated from monkeys and pigs and the H. mustelae urease from ferrets. The urease enzymes of each of these organisms were found to be of the same molecular weight. The urease enzyme of H. pylori consisted of two subunits of 68.2 and 31.3 kDa.