Oxidative activation of 2-aminofluorene by human red blood cell cytosol.
Purified red blood cell cytosol is able to activate 2-aminofluorene (2AF) to N-hydroxy-2-aminofluorene. Apparent kinetic parameters are determined with and without methylene blue. The latter, which maintains haemoglobin in the reduced form and stimulates NADPH production, increases the affinity of the enzyme for the 2AF. This activity is inhibited by carbon monoxide while cyanide is without effect. The involvement of a peroxidative reaction or a one-electron oxidative mechanism involving free radicals may be excluded.
Duverger-van Bogaert
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Laboratory TEMU, UCL/72.37, Brussels, Belgium.
Wiame
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Stecca
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C
D002248:Carbon Monoxide; D003600:Cytosol / Q000378:metabolism; D004789:Enzyme Activation; D004912:Erythrocytes / Q000378:metabolism*; D005449:Fluorenes / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008297:Male; D008751:Methylene Blue; D006899:Mixed Function Oxygenases / Q000378:metabolism
D005449:Fluorenes; C012177:2-aminofluorene; C001368:N-hydroxy-2-aminofluorene; D002248:Carbon Monoxide; D006899:Mixed Function Oxygenases; C035198:arylamine N-hydroxylase; D008751:Methylene Blue