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Echinobase
ECB-ART-39763
Proc Natl Acad Sci U S A 1984 Mar 01;815:1440-4. doi: 10.1073/pnas.81.5.1440.
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Tubulins from different higher plant species are immunologically nonidentical and bind colchicine differentially.

Morejohn LC , Bureau TE , Tocchi LP , Fosket DE .


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We have initiated immunological and drug-binding studies on the tubulins from different higher plant species. Antibodies were raised against electrophoretically separated rose (Rosa sp.) tubulin alpha- and beta-subunits and characterized by immunoblot autoradiographic assays. Each IgG preparation bound to its antigen and cross-reacted differentially with the respective tubulin subunits from an alga, sea urchin, rabbit, and cow. Antigenic determinants were shared more among the beta-subunits than among the alpha-subunits from these organisms. Tubulins were isolated from cultured cells of carrot (Daucus carota) and hibiscus (Hibiscus rosa-senensis). Immunoautoradiography and quantitation of cross-reactivity on blots showed nonidentity among homologous subunits from rose, carrot, hibiscus, and alga tubulins, with more antigenic differences among alpha-subunits than among beta-subunits. Comparative colchicine-binding assays showed that rose and hibiscus tubulins bound 33% and 65%, respectively, of the colchicine bound by carrot tubulin and that higher plant tubulins bound much less colchicine than bovine brain tubulin under identical conditions.

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Genes referenced: LOC100887844 tubgcp2

References [+] :
Asai, Two different monoclonal antibodies to alpha-tubulin inhibit the bending of reactivated sea urchin spermatozoa. 1982, Pubmed, Echinobase