Summary: The urease of (formerly ) has been partly purified by fast protein liquid chromatography. This material contained 10 nm doughnut-like structures when examined by electron microscopy and comprised three major polypeptides (61 kDa, 56 kDa and 28 kDa). Only two of these polypetides (61 kDa and 28 kDa) were observed in urese-containing material isolated by preparative non-denatured PAGE. Monoclonal antibodies (mAbs) were produced which were directed against two of these polypeptides (56 kDa and 28 kDa). Only mAbs directed against the 28 kDa polypetptide inhibited or captured urease activity. These results suggest that the 56 kDa polypeptide is not essential for anzyme actiity. Anti-urease mAbs were used in an indirect immunogold technique to localize the enzyme at the ultrastructural level. In both prefixed bacterial and ultrathin cryosectioned bacterial the enzyme was located on the cell surface and in material apparently shed from that surface.


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