December 17, 1998
Journal Article

Correlation between the Charge of Proteins in Solution and in the Gas Phase Investigated by Protein Charge Ladders, Capillary Electrophoresis, and Electrospray Ionization Mass Spectrometry

Abstract

Charge ladders of bovine carbonic anhydrase II, egg-white lysozyme, and bovine pacreatic trypsin inhibitor, prepared by partial acetylation of primary amino groups on the surface of the protein, have been analyzed by capillary electrophoresis (CE) and on-line electrospray ionization mass spectrometry (ESIMS) using solution conditions that maintain the native structure of the protein. Results demonstrate that the distrivution of charge states for proteins produced in the gas phase by ESI do not necessarily reflect the net charge of the protein in solution or the number of amino groups on the protein.

Revised: May 17, 2019 | Published: December 17, 1998

Citation

Carbeck J., J.C. Severs, J. Gao, Q. Wu, R.D. Smith, and G.M. Whitesides. 1998. Correlation between the Charge of Proteins in Solution and in the Gas Phase Investigated by Protein Charge Ladders, Capillary Electrophoresis, and Electrospray Ionization Mass Spectrometry. Journal of Physical Chemistry B 102, no. 51:10596-10601. PNNL-SA-30689. doi:10.1021/jp980768u