Immunochemical studies on purified common enterobacterial antigen (KUNIN).
A common antigen (KUNIN) purification method is described. The preparation obtained was highly antigenic, as proved by hemagglutination and its inhibition, and immunogenic in rabbits. Chemical analysis demonstrated the presence of an L-phosphoglycerid of the cephalin type, of protein, glucosamine, acetyl and glucose. The antigen had the character of an acidic polymer. It readily forms salt linkages with lysozyme. Phospholipase A induced the release of myristic, palmitic and stearic acids. It also destroyed both the antigenicity and immunogenicity of common antigen.
D000818:Animals; D000917:Antibody Formation / Q000187:drug effects; D000937:Antigen-Antibody Reactions / Q000187:drug effects; D000942:Antigens, Bacterial / Q000032:analysis / Q000302:isolation & purification; D011232:Chemical Precipitation; D004755:Enterobacteriaceae / Q000276:immunology*; D005227:Fatty Acids / Q000032:analysis; D005944:Glucosamine / Q000032:analysis; D005947:Glucose / Q000032:analysis; D006385:Hemagglutination Inhibition Tests; D006386:Hemagglutination Tests; D009113:Muramidase; D010740:Phospholipases / Q000494:pharmacology; D011817:Rabbits / Q000276:immunology
D000942:Antigens, Bacterial; D005227:Fatty Acids; D010740:Phospholipases; D009113:Muramidase; D005947:Glucose; D005944:Glucosamine