Stabilization of placental aromatase by dithiothreitol in the presence of oxidizing agents.
Cumene hydroperoxide, sodium periodate and iodosobenzene were not able to support aromatization by placental microsomes in the absence of NADPH or molecular oxygen. In the presence of these oxidizing agents and NADPH, aromatase was slowly inactivated. Dithiothreitol (10mM) prevented the loss of aromatizing activity in the presence of these compounds. One function of dithiothreitol may be to protect aromatase by scavenging harmful oxidizing agents.
D000332:Aerobiosis; D001141:Aromatase / Q000378:metabolism*; D004229:Dithiothreitol / Q000494:pharmacology*; D004355:Drug Stability; D005260:Female; D006801:Humans; D007700:Kinetics; D008861:Microsomes / Q000201:enzymology; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000378:metabolism*; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy
D010088:Oxidoreductases; D001141:Aromatase; D004229:Dithiothreitol