Biochemical Characterization of a Catalase Inhibitor from Maize 1
| Autor: | Sorenson, John C., Scandalios, John G. |
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| Jazyk: | angličtina |
| Rok vydání: | 1980 |
| Předmět: | |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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