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The Immobilization Antigens of Tetrahymena thermophila Are Glycoproteins
Author(s) -
RON ARIE,
WILLIAMS NORMAN E.,
DOERDER F. PAUL
Publication year - 1992
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.1550-7408.1992.tb04840.x
Subject(s) - tetrahymena , glycoprotein , mannose , glycan , antigen , glucosamine , phosphatidylinositol , immunoprecipitation , chemistry , biochemistry , microbiology and biotechnology , biology , membrane glycoproteins , gene , genetics , signal transduction
The four immobilization antigens controlled by the SerH locus in Tetrahymena thermophila have been isolated and partially characterized (Doerder, F. P. & Berkowitz, M. S. 1986. Purification and partial characterization of the H immobilization antigens of Tetrahymena thermophila. J. Protozool. , 33 :204–208). We show here, using immunoprecipitation and electrophoresis after labeling with 35 S‐methionine, 14 C‐mannose, 14 C‐glucosamine, and N‐Acetyl‐ d ‐[1‐ 3 H]glucosamine, that these proteins are glycosylated. We suggest the immobilization antigens in Tetrahymena may be anchored to the surface membrane by phosphatidylinositol glycans.