Plant Physiol. Drug Metab Dispos
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Plant Physiology 66:688-691 (1980)
© 1980 American Society of Plant Biologists

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Articles

Biochemical Characterization of a Catalase Inhibitor from Maize 1

John C. Sorenson and John G. Scandalios

Department of Genetics, North Carolina State University, Raleigh, North Carolina 27650

Some biochemical properties of the catalase inhibitor purified from maize scutella are described. The inhibitor is heat-labile and its activity is destroyed by trypsin, indicating that it is a protein. It does not appear to be a lectin nor does the inhibition involve proteolysis. The active inhibitor is a dimer with each subunit having a molecular weight of 5600 as determined by sodium dodecyl sulfate electrophoresis. A kinetic analysis performed in the presence of increasing levels of inhibitor gave unusual Lineweaver-Burk patterns. Possible explanations for these patterns are discussed. The inhibitor is active against all catalases tested from a wide variety of organisms.

1 This is Paper No. 5466 of the Journal Series of the North Carolina Agricultural Experiment Station, Raleigh. This work was supported by National Institutes of Health Grant GM 22733-01 (to J. G. S.).






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Copyright © 1980 by the American Society of Plant Biologists