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Purification And Partial Characterization Of Three Genetically Defined Catalases Of Maize
J. M. Chandlee, A. Tsaftaris, J. G. Scandalios
Published 1983 · Biology
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The purification of three genetically distinct catalase isozymes from Zea mays is described. These include CAT-1, CAT-2 and CAT-3 coded by the three distinct genetic loci Cat1, Cat2 and Cat3, respectively. The three purified isozymes were each subsequently characterized biochemically. All three isozymes contain subunits of similar molecular weight (Mr 60 000) giving the tetrameric catalase molecule a molecular weight of 240 000. The isozymes exhibit a pH optimum between 7 and 9. CAT-2 has the broadest range of pH stability with a maximum between pH 7–11. CAT-2 is stable at 45°C whereas CAT-1 and CAT-3 exhibit half-lives of 12.5 and 18 min, respectively, at that temperature. Overall, CAT-3 is most resistant to the various inhibitors tested (sodium azide, potassium cyanide, 3-amino-1,2,4-triazole (AT), β-mercaptoethanol (β-ME), dithiothreitol (DTT) and the endogenous maize catalase inhibitor). Each isozyme appears to be anti-genetically distinct as judged by immunodiffusion experiments.
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