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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Arachidonate 12-Lipoxygenase / biosynthesis
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Arachidonate 12-Lipoxygenase / genetics*
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Arachidonate 15-Lipoxygenase / genetics
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Arachidonate 5-Lipoxygenase / genetics
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Base Sequence
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Chromatography, High Pressure Liquid
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Cloning, Molecular
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DNA / biosynthesis
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DNA / chemistry
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Dimethyl Sulfoxide / pharmacology
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Gene Expression Regulation, Enzymologic*
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Genomic Library
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Humans
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Leukemia, Erythroblastic, Acute / enzymology*
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Molecular Sequence Data
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Open Reading Frames
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Restriction Mapping
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Tetradecanoylphorbol Acetate / pharmacology
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Tumor Cells, Cultured / drug effects
Substances
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DNA
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Arachidonate 12-Lipoxygenase
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Arachidonate 15-Lipoxygenase
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Arachidonate 5-Lipoxygenase
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Tetradecanoylphorbol Acetate
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Dimethyl Sulfoxide