H. pylori produces a urease (urea amidohydrolase; E,C. 184.108.40.206) that is interesting both from a biochemical as well as a functional standpoint.//, pylori urease is a multimeric complex composed of two repeating subunits that differs from most bacterial ureases, which have three subunits.1"4 Estimates for the molecular weight of the native enzyme have varied from between 380,000 to 680,000 Da.1'2-4"6 Purified H. pylori urease subunits have the capacity to form macromolecular aggregates that stack into either pairs or fours, and this may explain the variation in molecular weight determinations,7 Evidence suggest that H. pylori urease is predominantly associated with the periplasmic or outermembrane regions of the bacterial cell and that cellular components possessing urease activity can be easily extracted from cells.1"3-7 Hence it appears that H, pylori urease differs from most bacterial ureases which have been found to be cytoplasmically located.
|Title of host publication||Helicobacter pylori Biology and Clinical Practice|
|Editors||C. Stewart Goodwin|
|Place of Publication||Boca Raton USA|
|Number of pages||20|
|Publication status||Published - 1993|