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Updated: Jun 2, 2026
Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples
Published on: May 4, 2012
Characterization of oligosaccharides on methylcholanthrene-induced murine oncofetal antigen using biotinylated
L Gillis1, A Barsoum, S Gottlieb
1UNIV SO ALABAMA,DEPT BIOL SCI,MOBILE,AL 36688. UNIV SO ALABAMA,COLL MED,DEPT BIOCHEM,MOBILE,AL 36688. UNIV SO ALABAMA,COLL MED,DEPT MICROBIOL IMMUNOL,MOBILE,AL 36688. JO ELLEN SMITH MEM BAROMED RES INST,NEW ORLEANS,LA 70131.
Abstract:
Biotinylated lectins were used to characterize oligosaccharide chains of the minute amounts of the 44 kD membrane-bound oncofetal antigen (OFA) derived from murine MCA 1315 tumor cells. Lectins of known sugar specificity were used to detect oligosaccharides on glycoprotein which had been previously separated electrophoretically on sodium dodecyl sulfate polyacrylamide gels (SDS-PAGE) and blotted onto nitrocellulose (NC). Oligosaccharide reactivity with biotinlylated lectins was also analyzed after glycosidase treatment of the NC blotted OFA. Results indicate MCA 1315 derived OFA possesses N-glycosylated oligosaccharide chains which are high in mannose. This result is in agreement with the high mannose glycosylation of OFA derived from 13-day mouse fetuses.
