title: Biochemical characterization of a catalase inhibitor from maize.
abstract: 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.
authors: Department of Genetics, North Carolina State University, Raleigh, North Carolina 27650.
authors: J C
authors: JC
authors: Sorenson
authors: J G
authors: JG
authors: Scandalios