The immobilization antigens of Tetrahymena thermophila are glycoproteins.
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-[l-3H]glucosamine, that these proteins are glycosylated. We suggest the immobilization antigens in Tetrahymena may be anchored to the surface membrane by phosphatidylinositol glycans.
Ron
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A
Department of Anatomy and Embryology, Hebrew University-Hadassah Medical School, Jerusalem, Israel.
Williams
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NE
Doerder
F P
FP
D000818:Animals; D000953:Antigens, Protozoan / Q000737:chemistry*; D000954:Antigens, Surface / Q000737:chemistry*; D001345:Autoradiography; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000737:chemistry*; D015800:Protozoan Proteins; D016808:Tetrahymena thermophila / Q000737:chemistry*
D000953:Antigens, Protozoan; D000954:Antigens, Surface; D006023:Glycoproteins; D015800:Protozoan Proteins; C043323:immobilization antigens