Premium
Inducibility of arylhydrocarbon‐hydroxylase activity in human hair follicles by topical application of liquor carbonis detergens (coal tar)
Author(s) -
MERK H.,
RUMPF M.,
BOLSEN K.,
WIRTH G.,
GOERZ G.
Publication year - 1984
Publication title -
british journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.304
H-Index - 179
eISSN - 1365-2133
pISSN - 0007-0963
DOI - 10.1111/j.1365-2133.1984.tb04724.x
Subject(s) - pyrene , cytochrome , benzopyrene , enzyme , coal tar , chemistry , cytochrome p450 , in vivo , carcinogen , biochemistry , tar (computing) , substrate (aquarium) , microbiology and biotechnology , enzyme assay , benzo(a)pyrene , biology , coal , organic chemistry , genetics , ecology , computer science , programming language
Summary Arylhydrocarbon‐hydroxylase (AHH) is a cytochrome P‐450‐dependent polysubstrate mono‐oxygenase which plays an important role in converting some compounds (e.g. benzo[ a ]pyrene) to highly reactive carcinogenic species. A simple AHH assay is described, using [ 3 H]benzo[ a ]‐pyrene as substrate. 7,8‐Benzoflavone (10 ‐4 M) inhibits 92% of the measured enzyme activity. Liquor carbonis detergens (which contains coal tar) induces AHH activity in human hair follicles in vivo . We suggest that using this simple assay, hair follicles would be a very suitable tissue to test whether the AHH‐controlling gene is of significance in producing cancer.