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Hemoglobin variants as models for investigation of dissociation of intact polypeptide chains by ESI tandem mass spectrometry

Conference ·
OSTI ID:5736827
Electrospray ionization mass spectroscopy (ESI-MS) is rapidly becoming a practical biochemical tool for peptide and protein sequence analysis. The utility of ESI-MS is through use of Collisionally Activated Dissociation (ESI-CAD-MS). Human hemoglobin (Hb, {approximately}62 kDa) consists of four polypeptide chains and a prosthetic heme group. There are over 400 Hb variants, characterized by amino acid substitutions in either the alpha or beta polypeptide chains. We investigated ESI-CAD-MS as a tool for rapidly analyzing amino acid substitutions, using eight Hb beta chain variants. The approximate location of the modification can be deduced from comparison of the CAD mass spectra and observance of the mass shifts of the fragment ion containing the substitution. Fragmentation occurs preferentially at the amino terminus of proline residues. For most substitutions, differences in CAD mass spectra were not seen. 2 figs.
Research Organization:
Pacific Northwest Lab., Richland, WA (USA)
Sponsoring Organization:
DOE; USDOE, Washington, DC (USA)
DOE Contract Number:
AC06-76RL01830
OSTI ID:
5736827
Report Number(s):
PNL-SA-19121; CONF-9105181--29; ON: DE91015265
Country of Publication:
United States
Language:
English