以DHB/N,N-二甲基苯胺为基质使用MALDI LTQ Orbitrap质谱分析唾液酸化地糖链

简介:

In this study, we examined the utility of 2,5-dihydroxybenzoic acid/N,N-dimethylaniline(DHB/DMA) matrix11 to improve analysis of N-linked sialylated glycans from human α1-acid glycoprotein by MALDI.

仪器:

Thermo Scientific MALDI LTQ Orbitrap XL hybrid mass spectrometer

结论:

We have developed a simple, fast, and reliable workflow for profiling N-linked glycans. It combines the benefits of MALDI LTQ Orbitrap technology with the homogeneity of sample distribution throughout the crystal layer provided by the DHB/DMA matrix. The high mass accuracy and mass resolution provided by the Orbitrap detector enables confident structural discrimination without the aid of tandem MS. In addition, ions are produced with sufficient abundance for further characterization, if needed. The ability to profile both sialylated and asialylated glycans with a single ionization mode in MALDI experiments introduces a previously lacking practicality into the workflow. This ability is useful in determining the degree of silaylation relative to overall glycan composition. Finally, more glycans were identified and characterized using the DHB/DMA matrix, than the much studied DHB matrix.