Results 131 to 140 of about 263,945 (178)
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Genetic expression of aryl hydrocarbon hydroxylase activity in the mouse

Journal of Cellular Physiology, 1975
Monooxygenases require NADPH and molecular oxygen during the metabolism of numerous endogenous hydrophobic substrates and carcinogenic and toxic exogenous chemicals. The complexity of these membrane-bound multicomponent drug-metabolizing enzyme systems is reviewed.
Nebert, D W   +4 more
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Aryl hydroxylase induction in the chick embryo by polycyclic hydrocarbons

Biochimica et Biophysica Acta (BBA) - General Subjects, 1973
Abstract The ability of various polycyclic hydrocarbons to induce liver microsomal enzzmes which convert 7,12-[ 14 C ] dimethylbenz (a) anthracene to water-soluble products was compared in the chick embryo and the rat. A good correlation in response to the 18 hydrocarbons tested was obtained but the chick embryo was found to provide a
P H, Jellinck, G, Smith
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Pulmonary Carcinogenesis: Aryl Hydrocarbon Hydroxylase

1981
Especially during the past two decades, there has been a growing awareness that exposure of individuals to exogenous environmental agents is responsible for various kinds of cancer. Chemical carcinogenesis in man was first documented in 1775 by the British physician Percival Pott, who attributed the high incidence of scrotal cancer in London chimney ...
Theodore L. McLemore, R. Russell Martin
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Induction of aryl hydrocarbon hydroxylase activity and pulmonary carcinoma

International Journal of Cancer, 1979
AbstractAryl hydrocarbon hydroxylase activity in lymphoblasts from normal Finnish adults and from patients with pulmonary carcinomas and other types of malignancy has been studied by a modification of previously used techniques. High absolute induced aryl hydrocarbon hydroxylase activity was found in 39% of patients with untreated lung cancer but only ...
C G, Gahmberg   +4 more
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In Vitro Inhibition of Aryl Hydrocarbon Hydroxylase by Heavy Metals

Oncology, 2009
Inhibition of mouse hepatic aryl hydrocarbon hydroxylases (AHH), microsomal mixed-function oxidases was obtained with five bivalent metal chlorides. Concentrations ranged from 10––6 to 10––1 m. The enzyme system was induced by an intraperitoneal injection of a trioctanoin solution of 3-methylcholanthrene into C57B1/6J mice 24 hours before the hepatic ...
S, Tsang, A, Furst
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Aryl hydrocarbon hydroxylase in persons with lung or laryngeal cancer

International Journal of Cancer, 1978
AbstractTo test whether the distribution of AHH inducibility is shifted toward the high end of the range in patients who had lung and laryngeal cancer, we measured this trait in 59 patients (32 lung and 27 laryngeal) who had resectable tumors and had been disease‐free for a period of time.
Ward, E   +7 more
openaire   +2 more sources

Placental aryl hydrocarbon hydroxylase activity and placental calcifications

Toxicology, 1992
Induction of aryl hydrocarbon hydroxylase (AHH) activity in the placenta as a result of maternal exposure to polycyclic aromatic hydrocarbons contained in cigarette smoke has been well documented. Furthermore, calcifications are more prevalent in the placentas of pregnant smokers than in those of non-smokers.
G, Huel   +6 more
openaire   +2 more sources

Beryllium Effects on Aryl Hydrocarbon Hydroxylase in Rat Lung

Archives of Environmental Health: An International Journal, 1973
This study was undertaken to determine whether beryllium would interfere with pulmonary mixed function oxidases. Rats were injected intratracheally with 150 μmols/kg of a neutralized solution of beryllium sulfate (BeSO4). The activity of pulmonary aryl hydrocarbon hydroxylase (AHH) was measured one, two, and seven days, and two and four weeks after ...
A, Jacques, H R, Witschi
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Nuclear aryl hydrocarbon hydroxylase and interaction of polycyclic hydrocarbons with nuclear components

Archives of Biochemistry and Biophysics, 1977
Aryl hydrocarbon hydroxylase (AHH) activity has been demonstrated in the nucleus by a specific histofluorescent technique. The nuclear AHH is present at 15–20% of the activity of the microsomal enzyme. The properties of the nuclear and microsomal AHH have been compared.
E, Bresnick   +5 more
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Methylcholanthrene: A possible pseudosubstrate for adrenocortical 17α-hydroxylase and aryl hydrocarbon hydroxylase

Biochemical Pharmacology, 1986
In cultured bovine adrenocortical cells, loss of 17 alpha-hydroxylase activity was observed after incubation with 3-methylcholanthrene (3-MC). The suppression of 17 alpha-hydroxylase by 3-MC was rapid (50% loss of activity in 10 hr at 1 microM 3-MC), did not exhibit a lag period, and was not affected by cycloheximide. Direct effects of 3-MC on 17 alpha-
P J, Hornsby, K A, Aldern, S E, Harris
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