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Purification and Partial Characterization of the H Immobilization Antigens of Tetrahymena thermophila 1
Author(s) -
DOERDER F. P.,
BERKOWITZ M. S.
Publication year - 1986
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1986.tb05590.x
Subject(s) - tetrahymena , isoelectric focusing , antigen , chromatography , ammonium sulfate precipitation , size exclusion chromatography , fractionation , isoelectric point , chemistry , locus (genetics) , ammonium , molecular mass , biology , biochemistry , microbiology and biotechnology , gene , genetics , enzyme , organic chemistry
. 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.