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Purification and partial characterization of lipoxygenase with dual catalytic activities from human term placenta.
Results suggest that lipoxygenase from human term placenta exhibits both dioxygenase and hydroperoxidase activities, and this enzyme represents an important pathway for chemical oxidation in the placentas of non-smoking women. Expand
Direct Demonstration of Alterations in the Microcirculation of the Hamster during and following Renal Hypertension
The effects of norepinephrine (NE) on arterioles and venules and measured arteriolar wall (W) to lumen (L) ratios in the hamster cheek pouch were compared during the development of hypertension (HT)Expand
Placental peroxidase--further purification of the enzyme and oxidation of thiobenzamide.
Human term placental peroxidase from non-smoking women was purified by extraction of the membrane fraction with 0.5 M Ca2+ followed by affinity chromatography on concanavalin A, hydrophobic Chromatography on phenyl sepharose CL-4B and gel filtration chromatographyon sephacryl S-200 columns suggesting apparent homogeneity of the protein. Expand
Peroxidase: a novel pathway for chemical oxidation in human term placenta.
The results suggest that peroxidase may be a major enzyme in human term placenta capable of oxidation of endogenous chemicals and xenobiotics. Expand
Xenobiotic oxidation during early pregnancy in man: peroxidase catalysed chemical oxidation in conceptual tissues.
The results suggest that peroxidase may be one of the major pathways of xenobiotic oxidation present in organogenesis-stage human conceptual tissues influencing the toxicity of chemicals to which the developing embryo is exposed. Expand
Inhibition of human term placental and fetal liver glutathione-S-transferases by fatty acids and fatty acid esters.
The evidence suggests that Asc-S, Asc-P, SA and PA are potent inhibitors especially of the pi-class of GST. Expand
Peroxidative xenobiotic oxidation by partially purified peroxidase and lipoxygenase from human fetal tissues at 10 weeks of gestation.
The ability of partially purified peroxidase and lipoxygenase from human fetal tissues at 10 weeks of gestation to oxidize selected xenobiotics in vitro is reported to suggest thatperoxidases and lip oxygengenase may be important pathways for per oxidative xenobiotic oxidation in human fetal tissue. Expand
Bioactivation of benzo(a)pyrene-7,8-dihydrodiol catalyzed by lipoxygenase purified from human term placenta and conceptal tissues.
The results suggest that lipoxygenase in the placentas and intrauterine conceptal tissues is capable of metabolizing benzo(a)pyrene-7,8-dihydrodiol to several reactive metabolites and may represent one of the major xenobiotic metabolizing pathways of bioactivating chemicals in the intrautine compartment. Expand
2-Aminofluorene bioactivation by human term placental peroxidase.
The results strongly suggest that peroxidase may be one of the important pathways responsible for the bioactivation of arylamines in human term placenta. Expand
Subcellular heterogeneity in mitochondrial red-ox responses to KATP channel agonists in freshly isolated rabbit cardiomyocytes
The results are consistent with the view that mitochondria form independent functional units whose behaviour can be synchronised by some unknown cellular factors or metabolites. Expand