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Influences of pH and in-source collisional energy on the cationization of insulin
G Marie1, L Serani, O Laprévote
1Laboratorie de Spectrométrie de Masse, Institut de Chimie des Substances Naturelles, CNRS, Gifsur Yvette, France.
Rapid Communications in Mass Spectrometry : RCM
|September 16, 1998
Abstract:
The influence of pH and in-source collisional energy variations on interactions between a model protein and sodium or cesium ions has been studied by electrospray ionization mass spectrometry. Behavioural differences regarding cationization have been observed and seem to be linked to the neutral of deprotonated form of carboxylic acids. At pH 8, cesium and sodium adducts totally disappear in the case of highest charge states. Increasing the cone voltage leads to an overall change loss that can be attributed to the loss of cesium, sodium ions and even protons.