关键词: 糖基化肽, 卵清蛋白, 碰撞诱导裂解, 电子转移解离, 质谱

Abstract:

Identification of glycation sites in glycation protein plays an important role in the fields of food science and
medicine. In this work, liquid chromatography (LC) coupled with linear ion trap quadrupole-electrospray ionization tandem
mass spectrometry (LTQ-ESI CID/ETD MS-MS) was used to analyze peptides from glycated ovalbumin digested by pepsin.
The results indicated that primary identification of glycation peptides was carried out through CID MS spectrometry and site
identification through CID MS-MS fragment ions. However, new ion peaks from CID MS-MS analysis were very weak and
complex with some various degrees of neutral losses. ETD MS-MS was a technique more suitable for studying gaycated
peptide with medium molecular weight and 2 charges. Due to larger molecular gaycated peptides, it was hard to determine
the ETD fragments, so CID-NL-MS3 technique should be developed for the identification of the glycation site.

Key words: glycated peptide, ovalbumin, collision-induced dissociation (CID), electron transfer dissociation (ETD), MS