Antibodies raised against the Sarkosyl-insoluble, major flagellar glycoprotein fraction, mastigonemes, were used to determine the source of flagellar surface glycoproteins and to define the general properties of flagellar surface assembly in Euglena. After suitable absorption, mastigoneme antiserum reacts with several specific mastigoneme glycoproteins but does not bind either to the other major flagellar glycoprotein, xyloglycorien, or to other Sarkosyl-soluble flagellar components. When Fab' fragments of this mastigoneme-specific antiserum were used in combination with a biotin-avidin secondary label, antigen was localized not only on the flagellum as previously described but also in the contiguous reservoir region. If deflagellated cells are reservoir pulse-labeled with Fab' antibody, this antibody appears subsequently on the newly regenerated flagellum. This chased antibody is uniformly distributed throughout the length of the flagellum and shows no preferred growth zone after visualization with either fluorescein or ferritin-conjugated secondary label. From these and tunicamycin inhibition experiments it is concluded that (a) a surface pool of at least some flagellar surface antigens is present in the reservoir membrane adjacent to the flagellum and that (b) the reservoir antigen pool is transferred to the flagellar surface during regeneration.

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