Open AccessCharacterisation of the urease from Helicobacter pylori and comparison with the ureases from related spiral gastric bacteria
Author(s) -
Turbett G.R.,
Nandapalan N.,
Campbell I.G.,
Nikoletti S.M.,
Mee B.J.
Publication year - 1991
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1991.tb04158.x
Subject(s) - urease , helicobacter pylori , microbiology and biotechnology , monoclonal antibody , enzyme , bacteria , biology , epitope , helicobacter , chemistry , antibody , biochemistry , immunology , genetics
Summary 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.