title: Isolation and characterization of two antigens of Corynebacterium hofmannii.
abstract: Banach, T. M. (University of Manitoba, Winnipeg, Canada), and R. Z. Hawirko. Isolation and characterization of two antigens of Corynebacterium hofmannii. J. Bacteriol. 92:1304-1310. 1966.-A serologically active substance, extracted from sonically treated cells of Corynebacterium hofmannii with hot HCl, produced two precipitin lines by immunodiffusion tests with a hyperimmune homologous serum. Extracts of other species failed to precipitate with the hofmannii antiserum. The active fraction was eluted from a diethylaminoethyl cellulose column in the third adsorption peak at a linear concentration of 0.5 m KCl, and produced two precipitin lines which corresponded in identity to those formed by the acid extract. Separation of the antigens was achieved by rechromatography on a Sephadex G-200 column; the major antigen was designated A; the minor, B. The homogeneity and purity of each antigen was established by immunoelectrophoresis and, in addition, that of antigen A by disc electrophoresis. Biochemical analyses showed that both antigens were composed of a major protein component with polysaccharide and nucleic acid present in an approximate ratio of 17:3:1, respectively. Glutamic acid, aspartic acid, alanine, glycine, valine, and leucine were the main amino acids present. Antigen A contained 17% less protein and 3.5% less carbohydrate than antigen B. The principal sugars of antigen A were identified as arabinose and glucose. The molecular weight, estimated by gradient centrifugation, was 16,500 for antigen A and 21,000 for antigen B.
mesh_terms: D000596:Amino Acids; D000941:Antigens / Q000032:analysis*; D002845:Chromatography; D003352:Corynebacterium / Q000276:immunology*; D005779:Immunodiffusion; D007122:Immunoelectrophoresis; D008970:Molecular Weight; D013057:Spectrum Analysis; D014461:Ultracentrifugation
chemical_list: D000596:Amino Acids; D000941:Antigens