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Lipoxygenase (EC 1.13.11.12) from lupin seeds (Lupinus albus cv multolupa) was partially purified (38.4‐fold) by ammonium sulphate fractionation, hydrophobic chromatography and gel filtration. The enzyme was associated with membrane fragments of high particle weights. Its optimum pH was 6.1 and it had Km values for linoleic and linolenic acids of 0.24 and 0.37 mM, respectively. Molecular weight determination gave a value of 92000. Incubation of linoleic acid with partially purified enzyme afforded a mixture of 13‐hydroperoxy‐9cis, 11‐trans‐octadecadienoic and 9‐hydroperoxy‐10‐trans, 12‐cis‐octadecadienoic acids in which the ratio of isomers was 16:9.
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Olías et al. (1988) studied this question.
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