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Titlebook: Lipoxygenases and their Metabolites; Biological Functions Santosh Nigam,Cecil R. Pace-Asciak Book 1999 The Editor(s) (if applicable) and Th

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Molecular Cloning of a Second Human 15,-Lipoxygenase and its Murine Homologue, an 8,-Lipoxygenase,ppear to have distinct biological roles. The leukocyte 5S-lipoxygenase clearly functions in the initiation of a metabolic pathway; the leukotriene products have distinct cell receptors and mediate proin-flammatory activities. The platelet 12S lipoxygenase synthesizes 12.-HpETE, and following reducti
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Expression of Leukocyte-Type 12-Lipoxygenase and Reticulocyte-Type 15-Lipoxygenase in Rabbits,he rabbit 15-lipoxy-genase. HPLC product analysis of the bacterially expressed protein identified it as a leukocyte-type 12-lipoxygenase (1.12-LOX). This proves the co-expression of a 15-lipoxygenase and a 1.12-lipoxygenase in one mammalian species. Among the six amino acids that are different to ra
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Lipoxygenase Gene Disruption Studies,istinct from other lipoxygenase genes in its large size and its location on a separate chromosome (10q1 1.2 in humans and central chromosome 6 in mice) (1-5). A cluster of lipoxygenase genes located on mouse chromosome 11 (5,6) contains genes that encode three distinct 12(S)-lipoxy-genases, referred
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The Release of Polyunsaturated Fatty Acids and Their Lipoxygenation in the Brain,ydrolyze 20:4n6 and 22:6n3 equally well under both stimulated and basal conditions. Despite the high abundance of 22:6n3 in neuronal membranes, 20:4n6 is preferentially hydrolyzed from neuronal cells. These results suggest that 22:6n3 may be of more physiological importance in neuronal membranes as
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