Hunter A P, Games D E
Mass Spectrometry Research Unit, University of Wales Swansea, UK.
Rapid Commun Mass Spectrom. 1995;9(1):42-56. doi: 10.1002/rcm.1290090111.
Glycosylation sites in bovine alpha 1-acid glycoprotein (AGP) have been identified, and the inherent heterogeneity evaluated, by capillary electrophoretic and reversed-phase liquid chromatography/electrospray-mass spectrometric analyses of proteolytic digests of this glycoprotein. The success of these methods in locating glycopeptides relied on significant heterogeneity within each glycosylation site. In order to rapidly locate sites in glycoproteins of any degree of heterogeneity, a novel mass spectrometric method was applied to selectively identify the glycopeptides in a proteolytic digest of bovine alpha 1-AGP. The glycopeptides were selectively located by the generation and detection of characteristic oxonium ions from the carbohydrate moieties by collision-induced dissociation (CID) during liquid chromatography/electrospray-tandem mass spectrometry, and liquid chromatography/CID mass spectrometry, in which fragmentation was induced in the supersonic expansion region of the electrospray source.
通过对牛α1-酸性糖蛋白（AGP）蛋白水解消化产物进行毛细管电泳以及反相液相色谱/电喷雾质谱分析，已鉴定出该糖蛋白的糖基化位点，并评估了其内在异质性。这些方法在定位糖肽方面的成功依赖于每个糖基化位点内显著的异质性。为了快速定位任何异质性程度的糖蛋白中的位点，一种新型质谱方法被应用于选择性鉴定牛α1-AGP蛋白水解消化产物中的糖肽。在液相色谱/电喷雾串联质谱以及液相色谱/CID质谱分析中，通过碰撞诱导解离（CID）从碳水化合物部分产生并检测特征性鎓离子，从而选择性地定位糖肽，其中在电喷雾源的超声膨胀区域诱导裂解。
