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Electrospray analysis of proteins: A comparison of positive‐ion and negative‐ion mass spectra at high and low pH
Author(s) -
Kelly Michele A.,
Vestling Martha M.,
Fenselau Catherine C.,
Smith Philip B.
Publication year - 1992
Publication title -
organic mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 0030-493X
DOI - 10.1002/oms.1210271028
Subject(s) - chemistry , electrospray , lysozyme , myoglobin , ion , mass spectrum , mass spectrometry , cationic polymerization , chromatography , analytical chemistry (journal) , biochemistry , organic chemistry
Cationic and anionic electrospray mass spectra were measured for equine myoglobin, lactalbumin and hen egg white lysozyme from acidic and basic solutions. Both positive and negative ions were detected from all solutions in which the proteins were soluble. This was observed in both nebulization‐assisted and thermally assisted electrospray. As in other studies, the distribution of the charge states reflected functional groups in the proteins, and also folding or extension of the protein.