Previous work has indicated that ribosomes isolated from Salmonella typhimurium were highly immunogenic and afforded excellent protection against homologous challenge. Effective protection was obtained also when ribonucleic acid (RNA) extracted from these ribosomes was used as a vaccine. In this investigation ribosomes prepared by another method and washed repeatedly in 1 M NH4Cl lost much of their prophylactic potency and yielded poorly protective
A library of 22 hybridomas, which make antibodies to soluble wall antigens from the coleoptiles and primary leaves of etiolated corn (Zea mays L.) seedlings, was raised and cloned three times by limit dilution to assure monoclonal growth and stability. Two of these hybridomas made immunoglobulin G antibodies, designated mWP3 and mWP19, which both effectively immunoprecipitated peroxidase activity from crude and partially purified preparations of wall peroxidases. Direct peroxidase-binding assays revealed that both antibodies bound enzymes with peroxidase activity. As judged by immunoblot analyses, mWP3 recognized a Mr 98,000 wall peroxidase with an isoelectric point near 4.2, and mWP19 recognized a Mr 58,000 wall peroxidase. Immunogold localization studies showed both peroxidases are predominately in cell walls.
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