title: Purification and partial characterization of the H immobilization antigens of Tetrahymena thermophila.
abstract: The H immobilization antigens specified by the SerH locus of Tetrahymena thermophila have been purified by a procedure utilizing acid fractionation, ammonium sulfate precipitation, gel filtration, and ion exchange chromatography. Purified antigen migrates as a single band on SDS-PAGE and IEF. Molecular weights of the four allelic H antigens range from 44,000 to 52,000, and isoelectric points range from 4.1 to 4.5. No carbohydrate was detected.
mesh_terms: D000645:Ammonium Sulfate; D000818:Animals; D000953:Antigens, Protozoan / Q000032:analysis / Q000302:isolation & purification*; D000954:Antigens, Surface / Q000032:analysis / Q000302:isolation & purification*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008970:Molecular Weight; D015800:Protozoan Proteins; D013768:Tetrahymena / Q000032:analysis* / Q000276:immunology
chemical_list: D000953:Antigens, Protozoan; D000954:Antigens, Surface; D015800:Protozoan Proteins; C043323:immobilization antigens; D000645:Ammonium Sulfate