Porcine P2 myelin protein primary structure and bound fatty acids determined by mass spectrometry
2010 (English)In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 397, no 5, 1903-1910 p.Article in journal (Refereed) Published
Complementary collision-induced/electron capture dissociation Fourier-transform ion cyclotron resonance mass spectrometry was used to fully sequence the protein P2 myelin basic protein. It is an antigenic fatty-acid-binding protein that can induce experimental autoimmune neuritis: an animal model of Guillain-Barre syndrome, a disorder similar in etiology to multiple sclerosis. Neither the primary structure of the porcine variant, nor the fatty acids bound by the protein have been well established to date. A 1.8-angstrom crystal structure shows but a bound ligand could not be unequivocally identified. A protocol for ligand extraction from protein crystals has been developed with subsequent gas chromatography MS analysis allowing determination that oleic, stearic, and palmitic fatty acids are associated with the protein. The results provide unique and general evidence of the utility of mass spectrometry for characterizing proteins from natural sources and generating biochemical information that may facilitate attempts to elucidate the causes for disorders such as demyelination.
Place, publisher, year, edition, pages
2010. Vol. 397, no 5, 1903-1910 p.
CID, ECD, De novo sequencing, GC/MS, Lipid identification, Myelin proteins
Chemical Sciences Biological Sciences Medical and Health Sciences
IdentifiersURN: urn:nbn:se:uu:diva-136290DOI: 10.1007/s00216-010-3762-0ISI: 000278810000032PubMedID: 20512566OAI: oai:DiVA.org:uu-136290DiVA: diva2:376534
Erratum in: Analytical and Bioanalytical Chemistry, vol 398, issue 7-8, 2010, pages 3225-3226.
DOI: 10.1007/s00216-010-4204-82010-12-112010-12-112012-06-12Bibliographically approved