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Development and Growth Regulation

Monoclonal Antibodies Against Fusicoccin with Binding Characteristics Similar to the Putative Fusicoccin Receptor of Higher Plants ¹

Pflanzenphysiologie, Universität Osnabrück, Postfach 4469, D-4500 Osnabrück, Federal Republic of Germany

Monoclonal antibodies were raised against fusicoccin. The toxin, linked to bovine serum albumin through its t-pentenyl moiety, served as immunogen. Hybridomas secreting anti-fusicoccin antibodies were screened by radioimmunoassay employing a novel radioactive derivative, [³H]-nor-fusicoccin-alcohol of high specific activity (1.5 x 10¹⁴Bq/mole). The two monoclonal antibodies reported here are of high apparent affinity for fusicoccin (0.71 x 10^–9 molar and 1.85 x 10^–9 molar). This is comparable to the apparent affinity of rabbit antiserum raised against the same type of conjugate (9.3 x 10^–9 molar). A method for the single step purification of the monoclonal antibodies from ascites fluid is reported. A solid-phase immunoassay, using alkaline phosphatase as enzyme, exhibits a measuring range from 0.1 to 1.5 picomoles (about 70 picograms to 1 nanogram) of fusicoccin. The displacement of [³H]-nor-fusicoccin-alcohol from the antibodies by compounds structurally related to fusicoccin exhibits similar selectivity as a microsomal binding assay with the same tracer as radiolabeled probe.