Abstract
1. 1. Surface proteins of normal (bacterial endosymbiont-containing) and aposymbiotic Crithidia oncopelti and Blastocrithidia culicis were labeled with lactoperoxidase-catalyzed 125I, by NaB 3H 4 reduction following oxidation and by metabolic labelling with [ 3H]mannose and [ 3H]fucose. 2. 2. An intensely labelled diffuse band, detected after SDS-polyacrylamide gel electrophoresis and autoradiography of all labelled preparations, had a M r of about 30,000 and an isoelectric point of pH 7.0 3. 3. Aposymbiotic C. oncopelti failed to incorporate detectable amounts of [ 3H]fucose into the 30,000 M r species. 4. 4. Alterations in the fucose/mannose content of this major surface glycopeptide may help to explain previously reported differences between normal and aposymbiotic C. oncopelti in agglutinability by lectins.
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