Toward a simple, expedient, and complete analysis of human hemoglobin by MALDI-TOFMS

MALDI mass spectrometry is explored as a method for hemoglobin characterization. To simplify and expedite the analysis, hemoglobin is obtained without purification directly from whole human blood. The use of trypsinactivated bioreactive MALDI probes is evaluated as a means to further reduce the analysis time from hours to minutes. Moreover, variations of the MALDI matrix preparation facilitate detection of the problematic tryptic peptides alpha T12, alpha T13, and beta T12. The results reveal that MALDI-based methods are easily implemented, are rapid, and allow detection of traditionally elusive tryptic peptides.