Identification of N-acetylglucosamine-binding immunoglobulins in chicken egg yolk and serum distinct from the major mannose-binding immunoglobulins.
An N-acetyl-D-glucosamine (GlcNAc)-binding protein of 170 kDa has been isolated from hen serum and egg yolk. Another GlcNAc-binding protein of higher molecular mass was present only in the serum. The 170 kDa protein co-electrophoresed and co-chromatographed in gel filtration with a chicken IgG, and behaved identical to chicken IgG in double immunodiffusion with goat anti-chicken gamma chain antiserum. The sugar-binding hierarchy for the serum and yolk binding proteins, determined with bovine serum albumin neoglycoproteins, was GlcNAc greater than N-acetyl-D-galactosamine greater than glucose = galactose = L-fucose greater than mannose. This hierarchy was unlike any previously reported GlcNAc-binding proteins. The larger serum binding protein component was shown to be an IgM by double immunodiffusion with goat anti-chicken mu chain antiserum. The serum and yolk GlcNAc-binding proteins comprise a unique set of sugar-binding immunoglobulins distinct from the previously reported hen serum and yolk mannose-binding proteins (Wang et al., 1986).
Hoppe
C A
CA
Department of Biology, Johns Hopkins University, Baltimore, MD 21218.
Suzuki
H
H
Shih
J
J
Lee
Y C
YC
D000117:Acetylglucosamine / Q000378:metabolism*; D000818:Animals; D001667:Binding, Competitive; D002645:Chickens; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004530:Egg Yolk; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006027:Glycosides / Q000494:pharmacology; D005779:Immunodiffusion; D007074:Immunoglobulin G / Q000302:isolation & purification / Q000378:metabolism*; D007136:Immunoglobulins / Q000378:metabolism*; D007700:Kinetics; D008358:Mannose / Q000378:metabolism; D008970:Molecular Weight
D006027:Glycosides; D007074:Immunoglobulin G; D007136:Immunoglobulins; D008358:Mannose; D000117:Acetylglucosamine