## Abstract Electrospray ionization mass spectrometry (ESIβMS) has been used to characterize the denaturation of porcine hemoglobin (Hb) induced by solvent changes. This work provides evidence for the symmetric nature of Hb denaturation and demonstrates that heme losses from Ξ±β and Ξ²βmonomers occur
Observation of large subunit protein complexes by electrospray ionization mass spectrometry
β Scribed by Joseph A. Loo
- Publisher
- John Wiley and Sons
- Year
- 1995
- Tongue
- English
- Weight
- 431 KB
- Volume
- 30
- Category
- Article
- ISSN
- 1076-5174
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β¦ Synopsis
Abstract
Mass spectrometry with electrospray ionization and a magnetic sector instrument was used to detect multiply charged molecules for the nonβcovalently bound dimeric subunit protein complexes of horse liver alcohol dehydrogenase (M~r~ βΌ 80 000) and the tetrameric complexes of yeast alcohol dehydrogenase (M~r~ βΌ 147 000) and rabbit muscle pyruvate kinase (M~r~ βΌ 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.
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## Abstract An electrospray ionisation (ESI) mass spectrometric method for the determination of the equilibrium constant and free energy (Ξ__G__) of protein unfolding was used to monitor the denaturation process at different pH of three metalloβproteins, i.e. wildβtype copper azurin, zinc azurin an