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.
Full text
PDF



Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- CHANCE B., HERBERT D. The enzymesubstrate compounds of bacterial catalase and peroxides. Biochem J. 1950 Apr;46(4):402–414. doi: 10.1042/bj0460402. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HARGREAVES A. B., DEUTSCH H. F. The in vitro inhibition of catalase by a tumor factor. Cancer Res. 1952 Oct;12(10):720–726. [PubMed] [Google Scholar]
- HUNTER W. M., GREENWOOD F. C. Preparation of iodine-131 labelled human growth hormone of high specific activity. Nature. 1962 May 5;194:495–496. doi: 10.1038/194495a0. [DOI] [PubMed] [Google Scholar]
- Ho D. T., Scandalios J. G. Regulation of Alcohol Dehydrogenases in Maize Scutellum during Germination. Plant Physiol. 1975 Jul;56(1):56–59. doi: 10.1104/pp.56.1.56. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jolly S. O., Tolbert N. E. NADH-Nitrate Reductase Inhibitor from Soybean Leaves. Plant Physiol. 1978 Aug;62(2):197–203. doi: 10.1104/pp.62.2.197. [DOI] [PMC free article] [PubMed] [Google Scholar]
- KAMPSCHMIDT R. F. MECHANISM OF LIVER CATALASE DEPRESSION IN TUMOR-BEARING ANIMALS: A REVIEW. Cancer Res. 1965 Jan;25:34–45. [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Pressey R. Invertase inhibitors from red beet, sugar beet, and sweet potato roots. Plant Physiol. 1968 Sep;43(9):1430–1434. doi: 10.1104/pp.43.9.1430. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Quail P. H., Scandalios J. G. Turnover of genetically defined catalase isozymes in maize. Proc Natl Acad Sci U S A. 1971 Jul;68(7):1402–1406. doi: 10.1073/pnas.68.7.1402. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rupprecht M., Schleifer K. H. Comparative immunological study of catalases in the genus Micrococcus. Arch Microbiol. 1977 Jul 26;114(1):61–66. doi: 10.1007/BF00429631. [DOI] [PubMed] [Google Scholar]
- Scandalios J. G., Liu E. H., Campeau M. A. The effects of intragenic and intergenic complementation on catalase structure and function in maize: a molecular approach to heterosis. Arch Biochem Biophys. 1972 Dec;153(2):695–705. doi: 10.1016/0003-9861(72)90388-8. [DOI] [PubMed] [Google Scholar]
- Shainkin R., Birk Y. Alpha-amylase inhibitors from wheat. Isolation and characterization. Biochim Biophys Acta. 1970 Dec 22;221(3):502–513. doi: 10.1016/0005-2795(70)90221-7. [DOI] [PubMed] [Google Scholar]
- Sorenson J. C., Ganapathy P. S., Scandalios J. G. Regulation of maize catalase by changing rates of synthesis and degradation. Biochem J. 1977 Apr 15;164(1):113–117. doi: 10.1042/bj1640113. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sorenson J. C., Scandalios J. G. Developmental expression of a catalase inhibitor in maize. Plant Physiol. 1976 Mar;57(3):351–352. doi: 10.1104/pp.57.3.351. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sorenson J. C., Scandalios J. G. Purification of a catalase inhibitor from maize by affinity chromatography. Biochem Biophys Res Commun. 1975 Mar 3;63(1):239–246. doi: 10.1016/s0006-291x(75)80035-0. [DOI] [PubMed] [Google Scholar]
- Tsaftaris A. S., Sorenson J. C., Scandalios J. G. Glycosylation of catalase inhibitor necessary for activity. Biochem Biophys Res Commun. 1980 Feb 12;92(3):889–895. doi: 10.1016/0006-291x(80)90786-x. [DOI] [PubMed] [Google Scholar]
- Wallace W. Purification and properties of a nitrate reductase-inactivating enzyme. Biochim Biophys Acta. 1974 Mar 21;341(1):265–276. doi: 10.1016/0005-2744(74)90087-4. [DOI] [PubMed] [Google Scholar]

