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Macromolecular assembly of Helicobacter pylori urease investigated by mass spectrometry
Author(s) -
Pinkse Martijn W. H.,
Maier Claudia S.,
Kim JungIn,
Oh ByungHa,
Heck Albert J. R.
Publication year - 2003
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.443
Subject(s) - chemistry , dodecameric protein , urease , electrospray ionization , mass spectrometry , dissociation (chemistry) , supramolecular chemistry , helicobacter pylori , electrospray , biochemistry , combinatorial chemistry , biophysics , stereochemistry , crystallography , enzyme , chromatography , organic chemistry , crystal structure , dna , biology , medicine
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 corresponds to a dodecameric (αβ) 12 assembly of urease α (26 kDa) and β (61 kDa) subunits. The dodecamer disassembles readily into (αβ) 3 subunits in solution and under controlled collisional‐induced dissociation in the gas phase. This is in strong support of an ((αβ) 3 ) 4 architecture consistent with the recently published x‐ray structure. In vitro , the α and β subunits are capable of re‐assembling to (αβ) 3 , but not further to the dodecameric complex. Copyright © 2003 John Wiley & Sons, Ltd.