Immunological evidence to show that the N-acetylglucosaminidase and N-acetylgalactosaminidase activities of Dictyostelium discoideum reside in the same protein molecule.
Antibodies were produced against purified beta-N-acetylhexosaminidase from Dictyostelium discoideum. Ouchterlony tests produced a single precipitin band with both beta-N-acetylglucosaminidase and beta-N-acetylgalactosaminidase activities. Both activities were co-precipitated in exactly the same proportions in quantitative immunoprecipitation reactions. We conclude that one enzyme protein catalyses the hydrolysis of both N-acetylglucosaminides and N-acetylgalactosaminides.
D000118:Acetylglucosaminidase / Q000276:immunology / Q000378:metabolism*; D004023:Dictyostelium / Q000201:enzymology*; D000939:Epitopes; D006596:Hexosaminidases / Q000276:immunology* / Q000378:metabolism*; D005779:Immunodiffusion; D009235:Myxomycetes / Q000201:enzymology*
D000939:Epitopes; D006596:Hexosaminidases; D000118:Acetylglucosaminidase