The Immobilization Antigens of Tetrahymena thermophila Are Glycoproteins |
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| Authors: | ARIE RON NORMAN E. WILLIAMS F. PAUL DOERDER |
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| Affiliation: | Department of Anatomy and Embryology, The Hebrew University-Hadassah Medical School, Jerusalem 91010, Israel;Department of Biology, University of Iowa, Iowa City, Iowa 52242;Department of Biology, Cleveland State University, Cleveland, Ohio 44115 |
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| Abstract: | ABSTRACT 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 35S-methionine, 14C-mannose, 14C-glucosamine, and N-Acetyl- d -[1-3H]glucosamine, that these proteins are glycosylated. We suggest the immobilization antigens in Tetrahymena may be anchored to the surface membrane by phosphatidylinositol glycans. |
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| Keywords: | Cell surface membrane anchors |
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