Turnover of Genetically Defined Catalase Isozymes in Maize
- 1 July 1971
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences of the United States of America
- Vol. 68 (7), 1402-1406
- https://doi.org/10.1073/pnas.68.7.1402
Abstract
The turnover of two homotetramers of catalase, V(4) and Z(4), specified by genes at two separate loci, has been studied during germination of maize seed by the techniques of density labeling and starch-gel electrophoresis. Both isozymes were shown to be turning over during this time. However, Z(4) accumulates because the rate of synthesis exceeds the rate of degradation, whereas V(4) slowly disappears because the rate of degradation exceeds the rate of synthesis. Evidence is also presented that the rate of synthesis of Z(4) exceeds that of V(4), which suggests that this may be a major factor in the differential expression of the two catalase genes.Keywords
This publication has 11 references indexed in Scilit:
- Combined gradient-gel electrophoresis procedures for determining buoyant densities or sedimentation coefficients of all multiple forms of an enzyme simultaneouslyAnalytical Biochemistry, 1971
- Control of Enzyme Levels in Animal TissuesAnnual Review of Biochemistry, 1970
- Deuterium Oxide as a Density Label of Peroxidases in Germinating Barley EmbryosPlant Physiology, 1970
- Synthesis and inactivation of aminoacyl-transfer RNA synthetases during growth of Escherichia coliJournal of Molecular Biology, 1969
- Enzyme Induction in Higher PlantsScience, 1969
- A test for de novo synthesis of enzymes: density labeling with H2O18 of barley alpha-amylase induced by gibberellic acid.Proceedings of the National Academy of Sciences, 1967
- Determination of catalase activity by means of the Clark oxygen electrodeBiochimica et Biophysica Acta (BBA) - Enzymology, 1967
- PEROXIDASE ISOZYMES FROM HORSERADISH ROOTS .I. ISOLATION AND PHYSICAL PROPERTIES1966
- Subunit dissociation and recombination of catalase isozymes.Proceedings of the National Academy of Sciences, 1965
- Separation of labeled from unlabeled proteins by equilibrium density gradient sedimentationAnalytical Biochemistry, 1962