Results 301 to 310 of about 112,955 (338)
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Epidermal arachidonate lipoxygenase
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1983Guinea pig skin was found to display a high lipoxygenase activity, evidenced by the formation of a hydroxyeicosatetraenoic acid (HETE) from exogenous [14C]arachidonic acid. The lipoxygenase activity was localized to the epidermal layer of the skin, was completely inhibited by eicosatetraynoic acid (ETYA) and slightly enhanced by indomethacin ...
T, Ruzicka, A, Vitto, M P, Printz
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Prostaglandins & Other Lipid Mediators, 2002
Arachidonate 12-lipoxygenase introduces a molecular oxygen at carbon 12 of arachidonic acid to generate a 12-hydroperoxy derivative. The enzymes generate 12-hydroperoxy derivatives with either S- or R-configurations. There are three isoforms of 12S-lipoxygenases named after the cells where they were first identified; platelet, leukocyte and epidermis ...
Tanihiro, Yoshimoto +1 more
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Arachidonate 12-lipoxygenase introduces a molecular oxygen at carbon 12 of arachidonic acid to generate a 12-hydroperoxy derivative. The enzymes generate 12-hydroperoxy derivatives with either S- or R-configurations. There are three isoforms of 12S-lipoxygenases named after the cells where they were first identified; platelet, leukocyte and epidermis ...
Tanihiro, Yoshimoto +1 more
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Physiologia Plantarum, 1989
Lipoxygenases (EC 1.13.11.12), commonly found in plant tissues, catalyze peroxidation of polyunsaturated fatty acids to various primary and secondary oxidation products. Some of these products affect the aroma of foods and some may be of significance in plant growth and development and/or pest resistance.
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Lipoxygenases (EC 1.13.11.12), commonly found in plant tissues, catalyze peroxidation of polyunsaturated fatty acids to various primary and secondary oxidation products. Some of these products affect the aroma of foods and some may be of significance in plant growth and development and/or pest resistance.
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Proteins: Structure, Function, and Genetics, 1996
Lipoxygenases are a class of non-heme iron dioxygenases which catalyze the hydroperoxidation of fatty acids for the biosynthesis of leukotrienes and lipoxins. The structure of the 839-residue soybean lipoxygenase-1 was used as a template to model human 5-, 12-, and 15-lipoxygenases.
S T, Prigge +3 more
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Lipoxygenases are a class of non-heme iron dioxygenases which catalyze the hydroperoxidation of fatty acids for the biosynthesis of leukotrienes and lipoxins. The structure of the 839-residue soybean lipoxygenase-1 was used as a template to model human 5-, 12-, and 15-lipoxygenases.
S T, Prigge +3 more
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Theoretical and Applied Genetics, 1991
The copy number, genomic arrangement and linkage relationships of two classes of lipoxygenase gene have been investigated in Pisum(pea) lines. Each of the two classes contained two to three members in P. sativum lines. RFLPs associated with genomic fragments containing the 5' sequences of one gene class permitted its correlation in genetical analyses ...
C, Domoney +3 more
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The copy number, genomic arrangement and linkage relationships of two classes of lipoxygenase gene have been investigated in Pisum(pea) lines. Each of the two classes contained two to three members in P. sativum lines. RFLPs associated with genomic fragments containing the 5' sequences of one gene class permitted its correlation in genetical analyses ...
C, Domoney +3 more
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Lipoxygenases and leukotrienes
Journal of Allergy and Clinical Immunology, 1984Abstract Some characteristics of lipoxygenases in general and 5-lipoxygenases in particular are discussed.
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Journal of Lipid Mediators and Cell Signalling, 1995
In this article, it has been attempted to review data primarily on the activation of human 5-lipoxygenase, in vitro and in the cell. First, structural properties and enzyme activities are described. This is followed by the activating factors: Ca2+, membranes, ATP, and lipid hydroperoxide.
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In this article, it has been attempted to review data primarily on the activation of human 5-lipoxygenase, in vitro and in the cell. First, structural properties and enzyme activities are described. This is followed by the activating factors: Ca2+, membranes, ATP, and lipid hydroperoxide.
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