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    Biochem Biophys Res Commun. 1990 Nov 15;172(3):1230-5.

    Molecular cloning and expression of human arachidonate 12-lipoxygenase.

    Yoshimoto T, Yamamoto Y, Arakawa T, Suzuki H, Yamamoto S, Yokoyama C, Tanabe T, Toh H.

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    Department of Biochemistry, Tokushima University School of Medicine, Japan.

    Abstract

    The cDNA for a 12-lipoxygenase was isolated from cDNA library of human erythroleukemia cells. The cDNA had an open reading frame encoding 663 amino acids with a calculated molecular weight of 75,513. The deduced amino acid sequence of human 12-lipoxygenase exhibited 41.5%, 65.3% and 65.4% identity with human 5-lipoxygenase, human 15-lipoxygenase and porcine 12-lipoxygenase, respectively. Blot hybridization analysis of RNA from human erythroleukemia cells demonstrated a single species (3.1 kb) of mRNA with the cDNA probe for 12-lipoxygenase of these cells, but not with the cDNA for porcine leukocyte enzyme. The cytosol of Escherichia coli transformed with a recombinant pUC19 plasmid oxygenated the position 12 of arachidonic acid.

    PMID:
    2244907
    [PubMed - indexed for MEDLINE]

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