| Literature DB >> 17011785 |
V Lorenzi1, J Maury, J Casanova, L Berti.
Abstract
Lipoxygenase from olive fruit was purified to homogeneity for the first time after differential centrifugations and by hydrophobic chromatography. The enzyme had a molecular mass of 98 kDa and exhibited a maximal activity at pH 6. Lipoxygenase had a better affinity for linoleic acid (Km=82.44 microM) than for linolenic acid (Km = 306.26 microM). It is inhibited by linoleate:oxygen oxidoreductase (LOX) inhibitors like nordihydroguaiaretic acid (NDGA) or propyl gallate. The reaction product was 13-hydroperoxy octadecadienoic acid when linoleic acid was used as substrate.Entities:
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Year: 2006 PMID: 17011785 DOI: 10.1016/j.plaphy.2006.09.001
Source DB: PubMed Journal: Plant Physiol Biochem ISSN: 0981-9428 Impact factor: 4.270