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- W1552242073 abstract "Crystalline preparations of muconate lactonizing enzyme and muconolactone isomerase, two inducible enzymes that catalyze successive steps in the catechol branch of the β-ketoadipate pathway, were used to prepare antisera. Both enzymes were isolated from a strain of Pseudomonas putida biotype A. The antisera did not cross-react with enzymes of the same bacterial strain that catalyze the chemically analogous steps in the protocatechuate branch of the β-ketoadipate pathway, carboxymuconate lactonizing enzyme and carboxymuconolactone decarboxylase. The antisera gave heterologous cross-reactions of varying intensities with the muconate lactonizing enzymes and muconolactone isomerases of P. putida biotype B, P. aeruginosa, P. stutzeri , and all biotypes of P. fluorescens , but did not cross-react with the isofunctional enzymes of P. acidovorans , of P. multivorans , and of two bacterial species that belong to other genera. The evolutionary and taxonomic implications of the findings are discussed." @default.
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- W1552242073 date "1970-05-01" @default.
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- W1552242073 title "Comparative Immunological Studies of Two <i>Pseudomonas</i> Enzymes" @default.
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- W1552242073 doi "https://doi.org/10.1128/jb.102.2.351-362.1970" @default.
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