We report the identification of a novel, slightly unstable hemoglobin (Hb) variant [β12(A9)Thr → Pro; HBB: c.37A > C] that came to our attention during Hb A1C ion exchange chromatography where it migrated as a trailing shoulder on the Hb A0 peak. On electrospray ionization mass spectrometry (ESI MS), this electrophoretically silent variant was detected as an unresolved β component with a 2 Da decrease in average β chain mass.
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