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J Chromatogr B Biomed Sci Appl. 2000 Jan 14;737(1-2):203-12.

Purification of surface-associated urease from Helicobacter pylori.

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  • 1Department of Clinical Microbiology, Hygiene-Institute, University of Vienna, Austria. elmar.rokita@akh-wien.ac.at

Abstract

Helicobacter pylori colonizes the human gastric mucosa and produces large amounts of urease. The enzyme was extracted from the bacteria by distilled water and purified by gel-permeation (Sephacryl S-300), anion-exchange chromatography (Mono Q) and a second gel-permeation (Superdex 200). Urease enzyme activity was detected with a spectrophotometic assay based on phenol red. The optimal pH for anion-exchange was 6.9. The recovery of urease was 55-75%, purity 93-98% and the overall protein recovery 0.8-1.4%. The urease in the final extract still had enzymatic activity and showed the typical subunits of Mr 66000 and Mr 30000 when subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

PMID:
10681057
[PubMed - indexed for MEDLINE]
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