Macromolecular asserably of Helicobacter pylori urease investigated by mass spectrometry

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The supramolecular assembly of Helicobacter pylori urease was studied by nanoflow electrospray ionization orthogonal time-of-flight mass spectrometry. The measured molecular mass of the urease complex of 1.06 MDa corresponcts to a dodecameric (alphabeta)(12) assembly of urease alpha (26 kDa) and beta (61 kDa) subunits. The dodecamer disassembles readily into (alphabeta)(3) subunits in solution and under controlled collisional-induced dissociation in the gas phase. This is in strong support of an ((alphabeta)(3))(4) architecture consistent with the recently published x-ray structure. In vitro, the alpha and beta subunits are capable of re-assembling to (alphabeta)(3), but not further to.the dodecameric complex. Copyright (C) 2003 John Wiley Sons, Ltd.
Publisher
JOHN WILEY & SONS LTD
Issue Date
2003-03
Language
English
Article Type
Article
Keywords

APOPROTEIN COMPLEXES; PROTEIN ASSEMBLIES; PURIFICATION; ACTIVATION; SEQUENCE; ORIGIN; UREF; ESI

Citation

JOURNAL OF MASS SPECTROMETRY, v.38, no.3, pp.315 - 320

ISSN
1076-5174
DOI
10.1002/jms.443
URI
http://hdl.handle.net/10203/85640
Appears in Collection
BS-Journal Papers(저널논문)
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