Houston C T, Reilly J P
Department of Chemistry, Indiana University, Bloomington 47405, USA.
Anal Chem. 1999 Aug 15;71(16):3397-404. doi: 10.1021/ac990046e.
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.
基质辅助激光解吸电离质谱法（MALDI）被作为一种鉴定血红蛋白的方法进行研究。为了简化和加快分析过程，血红蛋白无需纯化，直接从全血中获取。对胰蛋白酶激活的生物活性MALDI探针的使用进行了评估，以此作为将分析时间从数小时进一步缩短至数分钟的一种手段。此外，MALDI基质制备方法的变化有助于检测有问题的胰蛋白酶肽αT12、αT13和βT12。结果表明，基于MALDI的方法易于实施、速度快，并且能够检测传统上难以捉摸的胰蛋白酶肽。
