Title of article
Affinities of various mammalian arachidonate lipoxygenases and cyclooxygenases for molecular oxygen as substrate
Author/Authors
Ivo Jur?nek، نويسنده , , Hiroshi Suzuki، نويسنده , , Shozo Yamamoto، نويسنده ,
Pages
10
From page
509
To page
518
Abstract
In an attempt to study affinities for molecular oxygen of mammalian arachidonate oxygenases, which remain unclarified at present, we determined activities of platelet-type 12-lipoxygenase, leukocyte-type 12-lipoxygenase, 5-lipoxygenase, 15-lipoxygenase, cyclooxygenase-1 and cyclooxygenase-2 at various oxygen concentrations. Activities of all the tested enzymes were assessed by oxygenation of radioactive arachidonic acid under hypoxic conditions, and part of the enzymes were also assayed by monitoring oxygen consumption. Their Km values for oxygen ranged between 10 and 26 μM. These results should be considered in investigations of arachidonic acid metabolism in pathophysiological processes associated with hypoxia.In an attempt to study affinities for molecular oxygen of mammalian arachidonate oxygenases, which remain unclarified at present, we determined activities of platelet-type 12-lipoxygenase, leukocyte-type 12-lipoxygenase, 5-lipoxygenase, 15-lipoxygenase, cyclooxygenase-1 and cyclooxygenase-2 at various oxygen concentrations. Activities of all the tested enzymes were assessed by oxygenation of radioactive arachidonic acid under hypoxic conditions, and part of the enzymes were also assayed by monitoring oxygen consumption. Their Km values for oxygen ranged between 10 and 26 μM. These results should be considered in investigations of arachidonic acid metabolism in pathophysiological processes associated with hypoxia.
Keywords
lipoxygenase , Cyclooxygenase , arachidonic acid , Km value for oxygen , hypoxia
Journal title
Astroparticle Physics
Record number
568141
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