3P-11 PDF
Methods for detecting protein complex ions in the presence of nonvolatile buffer by Native MS
The presence of salts and nonvolatile buffer components affects property of proteins such as the structure and the stability. However, these components cause suppression of ionization during electrospray ionization. It has long been suggested that ammonium acetate, one of volatile salts, is most suitable and commonly used for native mass spectrometry of the protein and protein complexes. In this study, to establish the methods appropriate for observation of the intact complex ions by native mass spectrometry from the protein solutions under the biochemical purification conditions, we examined the effects of ammonium acetate on detecting intact ions of protein complexes of ADH (protein complex) and nucleosome core particle (NCP, protein-DNA complex), prepared in Tris-HCl buffer.