Ct. Houston et Jp. Reilly, Toward a simple, expedient, and complete analysis of human hemoglobin by MALDI-TOFMS, ANALYT CHEM, 71(16), 1999, pp. 3397-3404
MALDI mass spectrometry is explored as a method for hemoglobin characteriza
tion. To simplify and expedite the analysis, hemoglobin is obtained without
purification directly from whole human blood. The use of trypsin-activated
bioreactive MALDI probes is evaluated as a means to further reduce the ana
lysis 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 a
re easily implemented, are rapid, and allow detection of traditionally elus
ive tryptic peptides.