Characterisation of the urease fromHelicobacter pyloriand comparison with the ureases from related spiral gastric bacteria

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-fike 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. INTRODUCTIONA wide range of mammalian species have been found to harbour spiral/helical bacteria within their stomachs.Animals known so far to be hosts for this type of organism include man [1], dogs, cats, rats [2], ferrets [3,4], pigs and monkeys [5];