Ref ID : 4212
F. Paul Doerder and M.S. Berkowitz; Purification and Partial Characterization of the H Immobilization Antigens of Tetrahymena thermophila. J.Protozool. 33(2):204-208, 1986
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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.