Hostname: page-component-78c5997874-lj6df Total loading time: 0 Render date: 2024-11-19T13:12:39.316Z Has data issue: false hasContentIssue false
  • English
  • Français

Detection of intact megaDalton protein assemblies of vanillyl-alcohol oxidase by mass spectrometry

Published online by Cambridge University Press:  01 March 2000

WILLEM J.H. VAN BERKEL ,
ROBERT H.H. VAN DEN HEUVEL ,
CEES VERSLUIS  and
ALBERT J.R. HECK
WILLEM J.H. VAN BERKEL
Affiliation:
Department of Biomolecular Sciences, Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands
ROBERT H.H. VAN DEN HEUVEL
Affiliation:
Department of Biomolecular Sciences, Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands
CEES VERSLUIS
Affiliation:
Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands
ALBERT J.R. HECK
Affiliation:
Department of Biomolecular Mass Spectrometry, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands
Get access

Abstract

Well-resolved ion signals of intact large protein assemblies, with molecular masses extending above one million Dalton, have been detected and mass analyzed using electrospray ionization mass spectrometry, with an uncertainty in mass of <0.2%. The mass spectral data seem to reflect known solution-phase behavior of the studied protein assembly and have therefore been directly used to probe the protein assembly topology and stability as a function of ionic strength and pH.

Keywords

electrospray ionization mass spectrometrynoncovalent interactionsprotein assembliesvanillyl-alcohol oxidase
Type
ACCELERATED COMMUNICATION
Information
Protein Science , Volume 9 , Issue 3 , March 2000 , pp. 435 - 439
Copyright
© 2000 The Protein Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)