N-糖酰胺酶F
聚糖
化学
糖基化
天冬酰胺
内糖苷酶
基质辅助激光解吸/电离
质谱法
糖蛋白
生物化学
苏氨酸
低聚糖
丝氨酸
外糖苷酶
质谱成像
N-连接糖基化
色谱法
酶
解吸
有机化学
吸附
作者
Richard R. Drake,Thomas W. Powers,Kim Norris‐Caneda,Anand Mehta,Peggi M. Angel
摘要
Abstract Glycosylation of cell surface, secreted, and circulating proteins is one of the most common types of post‐translational modification. These modifications occur most commonly as one of three major classes: N‐linked glycosylation on asparagine residues, O‐linked glycosylation on serine or threonine residues, or as glycosaminoglycan oligosaccharide polymers on serine. Specifically, for N‐linked glycans, an endoglycosidase enzyme, peptide N‐glycosidase F (PNGase F), cleaves the attached oligosaccharides between the asparagine and first sugar. A method to analyze released N‐glycans and map them to specific locations within a tissue is presented here. The PNGase F is applied by solvent sprayer as a molecular layer on frozen or formalin‐fixed tissues and all released N‐glycans in a given region of tissue are detected using matrix‐assisted laser desorption/ionization (MALDI) imaging mass spectrometry (MALDI‐IMS). Using the described MALDI‐IMS protocol, at least 40 or more individual N‐glycans can be mapped to tissue histopathology and extracted for further structural analysis approaches. © 2018 by John Wiley & Sons, Inc.
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