Application of high-precision isotope ratio monitoring mass spectrometry to identify the biosynthetic origins of proteins.
Isotope ratio monitoring (IRM) mass spectrometry was used to measure the relative abundance of stable isotopes in several samples of adult human hemoglobin expressed in E. coli, yeast, and human blood. The results showed significant differences in the distribution of (15)N and (13)C isotopes among hemoglobin samples produced in these organisms. This indicates that IRM mass spectrometry can be used in forensic protein chemistry to identify the origin of protein expression.
Apostol
I
I
Baxter Hemoglobin Therapeutics, Boulder, Colorado 80301, USA. iapostol@amgen
Brooks
P D
PD
Mathews
A J
AJ
D000818:Animals; D001769:Blood / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D005554:Forensic Medicine; D006454:Hemoglobins / Q000032:analysis / Q000737:chemistry; D006801:Humans; D007554:Isotopes / Q000032:analysis; D013058:Mass Spectrometry / Q000379:methods; D011506:Proteins / Q000032:analysis* / Q000737:chemistry; D012015:Reference Standards; D013045:Species Specificity; D015003:Yeasts / Q000378:metabolism
D006454:Hemoglobins; D007554:Isotopes; D011506:Proteins