Factors affecting product specificity of peanut lipoxygenase.
Explore the source record for details and available documents.
Arachis↗
Biomedical subjects
H E Pattee
Publications and source records attributed to H E Pattee.
Peanut alkaline lipase.
Peanut alkaline lipase, (glycerol ester hydrolase EC 3.1.1.3), pH optimum 8.5, was isolated from acetone powders prepared from developing and germinated peanut seed (arachis hypogaea L. var. NC-2). Enzyme activity/seed increased in successive developmental stages. The course of the hydrolytic reaction was linear with regard to enzyme concentration and all times tested up to periods exceeding 60 min. Km for the reaction was determined to be 2.6 times 10-4M. Molecular weight of peanut lipase, as estimated by Sephadex gel filtration and sodium dodecyl sulfate gel electrophoresis, was ca. 55,000.
Ammonium Sulfate↗
Aerobic pentane production by soybean lipoxygenase isozymes.
The effects of oxygen on production of pentane and compounds absorbing at 234 nm and 285 nm by soybean lipoxygenase isozymes I and II were examined in a model system. Aerobic conditions increased pentane production. Differences in dienone formation (A285) and diene conjugation (A234) indicate the reaction sequences of the 2 isozymes are not the same.
Aerobiosis↗
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.
Arachis↗