title: The demonstration of nickel in the urease of Helicobacter pylori by atomic absorption spectroscopy.
abstract: Fast protein liquid chromatography and SDS-PAGE have been used to isolate and purify Helicobacter pylori urease. A nickel component of the urease was detected in the purified proteins by atomic absorption spectroscopy. The nickel was present only in the 61 kDa polypeptide and in the ratio of between five and six atoms to one molecule of urease, suggesting a hexameric structure. These results are discussed in relation to other bacterial ureases and urease activity at low pH.
authors.affiliation: PHLS, Southampton General Hospital, U.K.
authors.forename: P R
authors.initials: PR
authors.lastname: Hawtin
authors.forename: H T
authors.initials: HT
authors.lastname: Delves
authors.forename: D G
authors.initials: DG
authors.lastname: Newell
mesh_terms: D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D016480:Helicobacter pylori / Q000201:enzymology*; D009532:Nickel / Q000737:chemistry*; D013054:Spectrophotometry, Atomic; D014510:Urease / Q000302:isolation & purification*
chemical_list: D009532:Nickel; D014510:Urease