Abstract
Electrospray ionization – ion mobility spectrometry – mass spectrometry (ESI–IMS–MS) allows the identification of protein polymorphic distribution of protein conformers and oligomers. We report the detailed identification of the species observed with commercially available pharmaceutical preparation of wild-type, regular human insulin.
Highlights
Electrospray ionization – ion mobility spectrometry – mass spectrometry (ESI–IMS–MS) allows the identification of protein polymorphic distribution of protein conformers and oligomers
Electrospray ionization - mass spectrometry coupled to ion mobility spectrometry measurements of regular-acting human insulin measured in ammonium acetate
Electrospray ionization mass-spectrometry coupled to ion-mobility spectroscopy (ESI–IMS–MS)
Summary
Assignment of polymorphic species of insulin analogues in ion mobility mass spectroscopy Maely P. Sa. das Graças, 50 - Xerém, Duque de Caxias 25250-020, Rio de Janeiro, Brazil c National Institute of Science and Technology for Structural Biology and Bioimaging (INBEB-INCT), Federal University of Rio de Janeiro, Rio de Janeiro 21941-590, Brazil d Brazilian National Cancer Institute (INCA), 20230-014 Rio de Janeiro, RJ, Brazil e Department of Chemistry, Institute of Exact Sciences, Rural Federal University of Rio de Janeiro - UFRRJ, Rodovia BR 465, km 7, CEP:23890-000 Seropédica, RJ, Brazil article info. Electrospray ionization – ion mobility spectrometry – mass spectrometry (ESI–IMS–MS) allows the identification of protein polymorphic distribution of protein conformers and oligomers. We report the detailed identification of the species observed with commercially available pharmaceutical preparation of wild-type, regular human insulin.
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