Characterisation of horse dander allergen glycoproteins using amino acid and glycan structure analyses. a mass spectrometric method for glycan chain analysis of glycoproteins separated by two-dimensional electrophoresis.

摘要: Separation of horse dander allergens using two-dimensional PAGE resulted in the identification 16 proteins that react with allergic patient sera. A sensitive method has been developed for analysing structures glycan chains individual glycoprotein transferred to blots following PAGE, and allowed structural most abundant isoforms Equ c 1, a glycosylated major allergen. The involves separation by transfer polyvinylidene difluoride membranes, release peptide N-glycosidase F, permethylation mass spectrometric analysis derivatised glycans. amino acid compositions separated have determined, allowing various 1. These results also confirmed two non-glycosylated allergens, 2.0101 2.0102, belong lipocalin family, support idea these are probably same protein. identified common biantennary triantennary chains. carbohydrate moieties may role binding IgE; however, it is more likely overall structure involving both protein moieties, rather than alone, responsible eliciting responses.