✍ Scribed by Martijn W. H. Pinkse; Claudia S. Maier; Jung-In Kim; Byung-Ha Oh; Albert J. R. Heck
No coin nor oath required. For personal study only.
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.
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