ABSTRACT

I. INTRODUCTION Increasingly, glycosylation on proteins has been found to be important for stability, secretion, biological activity, and cell-cell and cell-extracellular ma­ trix interactions [1]. Despite recognition of the importance of glycosylation, rarely are specific sites of glycosylation assigned, and usually only the pooled oligosaccharides from the protein are characterized [2]. This leads to the loss of positional information such as the identification of the in vivo ac­ ceptor site specificity of a particular glycosyltransferase, whether there is sitespecific heterogeneity, and how much sugar is at each site of glycosylation.