Antibodies that recognize phosphodiester-linked amino-N-acetylglucosamine-1-phosphate residues.
An affinity chromatography procedure was developed for isolating antibodies that recognized phosphodiester-linked alpha-N-acetylglucosamine-1-phosphate (alpha-GlcNAc-1-P) residues. The affinity resin consisted of uridine-5'-diphospho-alpha-N-acetylglucosamine (UDPGlcNAc) conjugated to Sepharose. Antiserum prepared against Proteinase 1 from the cellular slime mold, Dictyostelium discoideum was used as a source of the anti-alpha-GlcNAc-1-P antibodies. Immunoblot assays showed that the affinity-isolated antibodies recognized phosphoglycosylated subunits of Proteinase 1, and that UDPGlcNAc blocked this interaction.
Department of Microbiology, University of Montana, Missoula 59812.
D J
DJ
Finn
G L
GL
Gustafson
D000117:Acetylglucosamine / Q000031:analogs & derivatives / Q000276:immunology*; D000906:Antibodies / Q000302:isolation & purification; D000936:Antigen-Antibody Complex; D000941:Antigens; D002846:Chromatography, Affinity; D005944:Glucosamine / Q000031:analogs & derivatives*; D007074:Immunoglobulin G; D046911:Macromolecular Substances; D014537:Uridine Diphosphate N-Acetylglucosamine
D000906:Antibodies; D000936:Antigen-Antibody Complex; D000941:Antigens; D007074:Immunoglobulin G; D046911:Macromolecular Substances; D014537:Uridine Diphosphate N-Acetylglucosamine; C026146:N-acetylglucosamine-1-phosphate; D005944:Glucosamine; D000117:Acetylglucosamine