Lipoxygenase isozymes of peanut.
Lipoxygenase was isolated and partially purified from peanut seed by ammonium sulfate precipitation, gel filtration, and ion exchange column chromatography. Three isozymes of lipoxygenase were identified. Two had pH optima of 6.2, and the other an optimum of 8.3. Molecular weight of each isozyme was 7.3 x 10(4), as determined by gel filtration. The alkaline optimum isozyme was not inhibited by NaCN and was inhibited by CaCl2 except at very low concentrations. The acid optimum isozymes were inhibited by NaCN and were stimulated by CaCl2 concentrations up to ca. 0.7 mM.
Lipoxygenase isozymes of peanut. Lipoxygenase was isolated and partially purified from peanut seed by ammonium sulfate precipitation, gel filtration, and ion exchange column chromatography. Three isozymes of lipoxygenase were identified. Two had pH optima of 6.2, and the other an optimum of 8.3. Molecular weight of each isozyme was 7.3 x 10(4), as determined by gel filtration. The alkaline optimum isozyme was not inhibited by NaCN and was inhibited by CaCl2 except at very low concentrations. The acid optimum isozymes were inhibited by NaCN and were stimulated by CaCl2 concentrations up to ca. 0.7 mM.