Abstract
In this study, we combined affinity labeling with glycosidase treatments in order to characterize the oligosaccharide moieties of VIP receptors from the human cell line IGR39, human and rat intestinal cells, and pig and rat liver. When using various non cleavable crosslinking reagents, BSOCOES was the most efficient in promoting VIP receptor labeling. Apparent molecular weights of major 125 I-VIP-labeled components were heterogenous, ranging from Mr=52,700 to 67,800. Treatment with peptide-N'-(N-acetyl-β-D-glucosaminyl) asparagine amidase (PNGase F), which hydrolyses the glycosamine linkage of N-glycoproteins, resulted in a strong decrease of heterogeneity
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