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Application of high‐precision isotope ratio monitoring mass spectrometry to identify the biosynthetic origins of proteins
Author(s) -
Apostol Izydor,
Brooks Paul D.,
Mathews Antony J.
Publication year - 2001
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.90101
Subject(s) - mass spectrometry , isotope , hemoglobin , chemistry , natural abundance , stable isotope ratio , isotope ratio mass spectrometry , abundance (ecology) , stable isotope labeling by amino acids in cell culture , chromatography , proteomics , analytical chemistry (journal) , biochemistry , biology , ecology , physics , quantum mechanics , gene
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.