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Observation of large subunit protein complexes by electrospray ionization mass spectrometry
Author(s) -
Loo Joseph A.
Publication year - 1995
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.1190300127
Subject(s) - chemistry , mass spectrometry , electrospray ionization , alcohol dehydrogenase , protein subunit , chromatography , electrospray , sample preparation in mass spectrometry , molecule , protein mass spectrometry , alcohol , biochemistry , organic chemistry , gene
Mass spectrometry with electrospray ionization and a magnetic sector instrument was used to detect multiply charged molecules for the non‐covalently bound dimeric subunit protein complexes of horse liver alcohol dehydrogenase ( M r ∼ 80 000) and the tetrameric complexes of yeast alcohol dehydrogenase ( M r ∼ 147 000) and rabbit muscle pyruvate kinase ( M r ∼ 232 000). Ions for the pyruvate kinase complex represent one of the largest intact protein complexes resolved by mass spectrometry. Solvation of the large gas phase complexes is indicated by the mass spectrometric results.