As mentioned above, lectins are
nonimmunological proteins that bind carbohydrate motifs. They can have either broad or narrow
specificities, and even the most promiscuous of lectins, such as the plant lectin concanavalin A
(ConA) from jackbean, binds only a defined portion of the glycome, which biases the analysis
in favor of the related glycoprotein fraction (Figure 7). To solve this problem, multiple lectins
can be used to isolate a wider swath of the glycome (48). A recent variation of this technique
was used by Mann and colleagues (12) to study the entire mouse N-glycoproteome. In this study,
As mentioned above, lectins arenonimmunological proteins that bind carbohydrate motifs. They can have either broad or narrowspecificities, and even the most promiscuous of lectins, such as the plant lectin concanavalin A(ConA) from jackbean, binds only a defined portion of the glycome, which biases the analysisin favor of the related glycoprotein fraction (Figure 7). To solve this problem, multiple lectinscan be used to isolate a wider swath of the glycome (48). A recent variation of this techniquewas used by Mann and colleagues (12) to study the entire mouse N-glycoproteome. In this study,
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