Lipoxygenase isozymes of peanut

descriptionPublicationkeyboard_double_arrow_right Article 01 Nov 1975 English Publisher:WileyJournal:Lipids, volume 10, pages 681-685 (issn: 0024-4201, eissn: 1558-9307,

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Authors: T H, Sanders; H E, Pattee; J A, Singleton;

doi: 10.1007/bf02532761

pmid: 580

Lipoxygenase isozymes of peanut

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Abstract

AbstractLipoxygenase 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 7.3×104, 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.

Related Organizations

North Carolina State University
United States
North Carolina Agricultural and Technical State University
United States

Keywords

Isoenzymes, Molecular Weight, Calcium Chloride, Kinetics, Cyanides, Arachis, Lipoxygenase, Hydrogen-Ion Concentration, Plants

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