Affinities of various mammalian arachidonate lipoxygenases and cyclooxygenases for molecular oxygen as substrate

Citation
I. Juranek et al., Affinities of various mammalian arachidonate lipoxygenases and cyclooxygenases for molecular oxygen as substrate, BBA-MOL C B, 1436(3), 1999, pp. 509-518
Citations number
41
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
ISSN journal
13881981 → ACNP
Volume
1436
Issue
3
Year of publication
1999
Pages
509 - 518
Database
ISI
SICI code
1388-1981(19990104)1436:3<509:AOVMAL>2.0.ZU;2-N
Abstract
In an attempt to study affinities for molecular oxygen of mammalian arachid onate oxygenases, which remain unclarified at present, we determined activi ties of platelet-type 12-lipoxygenase, leukocyte-type 12-lipoxygenase, 5-li poxygenase, 15-ljpoxygenase, cyclooxygenase-1 and cyclooxygenase-2 at vario us oxygen concentrations. Activities of all the tested enzymes were assesse d by oxygenation of radioactive arachidonic acid under hypoxic conditions, and part of the enzymes were also assayed by monitoring oxygen consumption. Their K-m values for oxygen ranged between 10 and 26 mu M. These results s hould be considered in investigations of arachidonic acid metabolism in pat hophysiological processes associated with hypoxia. (C) 1999 Elsevier Scienc e B.V. All rights reserved.