Results 131 to 140 of about 3,554 (178)

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.
M J, Finnen, C M, Lawrence, S, Shuster
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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.
M W, Kahng, W, Liu, H, Sanefuji, J H, Resau, B M, Heatfield, B F, Trump   +5 more
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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 ...
M J, Finnen, S, Shuster, C M, Lawrence, M D, Rawlins   +3 more
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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.
G, Kellermann, C R, Shaw, M, Luyten-Kellerman   +2 more
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Aryl Hydrocarbon Hydroxylase Inducibility in Laryngeal Carcinoma

Archives of Otolaryngology - Head and Neck Surgery, 1978
The chief carcinogens of tobacco smoke--the polycyclic aromatic hydrocarbons--must be activated in the cells to exert their carcinogenic effect. This activation is carried out by the enzyme system aryl hydrocarbon hydroxylase (AHH). Mitogen-stimulated, human lymphocyte studies of AHH activity indicate wide individual variation, which is under strict ...
J H, Brandenburg, G, Kellermann
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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 ...
C S, Yang, F S, Strickhart, L P, Kicha
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Aryl Hydrocarbon Hydroxylase Induction in Human Leukocytes

Science, 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.
D L, Busbee, C R, Shaw, E T, Cantrell
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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.
J C, Nunnink, A H, Chuang, E, Bresnick
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Aryl Hydrocarbon Hydroxylase: Induction

1977
Knowledge about the enzyme system responsible for the metabolism of aryl hydrocarbons dates back to the early studies of Conney et al. (1), who showed the enzyme(s) responsible for the oxidation of benzpyrene to be located in the microsomal fraction of the liver. In that study it was shown that the enzyme system required both NADPH and molecular oxygen
John B. Schenkman, Kathy M. Robie, Ingela Jansson   +2 more
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