Results 121 to 130 of about 17,003 (187)
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In Vitro Inhibition of Aryl Hydrocarbon Hydroxylase by Heavy Metals

Oncology, 1976
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
A. Furst, Sophia Tsang
openaire   +4 more sources

Aryl Hydrocarbon Hydroxylase Inducibility and Bronchogenic Carcinoma

New England Journal of Medicine, 1973
Abstract Aryl hydrocarbon hydroxylase is an inducible, membrane-bound enzyme involved in the metabolism of chemical carcinogens. In cultured human lymphocytes there is genetic variation.
Mieke Luyten-Kellerman   +2 more
openaire   +4 more sources

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
openaire   +4 more sources

Aryl Hydrocarbon Hydroxylase Induction in Human Leukocytes [PDF]

open access: possibleScience, 1972
A method for determining aryl hydrocarbon hydroxylase induction in human leukocytes is described. Leukocytes from healthy volunteers were cultured in the presence of phytohemagglutinin, a mitogen. Addition of 3-methylcholanthrene to 72-hour cultures induced a fourfold increase in aryl hydroxylase activity.
E. T. Cantrell, C. R. Shaw, D. L. Busbee
openaire   +2 more sources

Analysis of the aryl hydrocarbon hydroxylase assay

Biochemical Pharmacology, 1978
Abstract The assay method and the properties of aryl hydrocarbon hydroxylase were studied with rat liver microsomes. The assay could be carried out by two methods: (1) the microsomes (initially at 15–20°) were pre-incubated at 37° and then benzo[a]pyrene and NADPH were added to initiate the assay; and (2) benzo[a]pyrene was added to microsomes at 15 ...
Chung S. Yang   +2 more
openaire   +3 more sources

Enhanced metabolic activation of chemical hepatocarcinogens in woodchucks infected with hepatitis B virus.

Carcinogenesis, 1989
The metabolism of chemical carcinogens was investigated in liver preparations from 28 captive woodchucks (Marmota monax). Of these, 23 were naturally infected with the woodchuck hepatitis virus (WHV), and eight also had primary hepatocellular carcinoma ...
S. Flora   +6 more
semanticscholar   +1 more source

Human skin aryl hydrocarbon hydroxylase

British Journal of Dermatology, 1984
Aryl hydrocarbon hydroxylase (AHH) activity has been measured in full-thickness biopsies of human skin from patients with and without psoriasis. Basal levels of enzyme activity varied over a fivefold range and were not related to age, sex or clinical condition.
Clifford M. Lawrence   +2 more
openaire   +3 more sources

Aryl hydrocarbon hydroxylase in human prostate

Chemico-Biological Interactions, 1981
Aryl hydrocarbon hydroxylase (AHH) was present in explant cultures of human prostate obtained from surgery of benign prostatic hyperplasia and was inducible by benz[a]anthracene (BA). The induction of AHH ranged from 14- to 150-fold when compared with control values and 10-fold variation of AHH inducibility among individuals was observed.
Wing Liu   +5 more
openaire   +3 more sources

Aryl hydrocarbon hydroxylase activity and psoriasis

Biochemical Pharmacology, 1983
Aryl hydrocarbon hydroxylase (AHH) has been measured in the skin, jejunum and liver of normal and psoriatic individuals. We have been unable to confirm previous reports of an abnormality in AHH activity in patients with psoriasis. Re-examination of the laboratory records on which the original reports were based leads us to doubt their veracity and ...
Cliff M. Lawrence   +3 more
openaire   +3 more sources

The ontogeny of nuclear aryl hydrocarbon hydroxylase

Chemico-Biological Interactions, 1978
The ontogeny of rat liver nuclear aryl hydrocarbon hydroxylase (AHH) ws studied. AHH which was barely detectable in 18--20 day fetal rat liver nuclei increased rapidly post-partum reaching a value which was over 200 times greater than the fetal liver specific activity.
Edward Bresnick   +2 more
openaire   +3 more sources

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