Subcellular distribution of aromatase in human placenta and ovary.
The aromatization of androstenedione in human ovarian microsomes is inhibited by an antibody to porcine hepatic microsomal NADPH-cytochrome c reductase. Likewise, the antibody inhibits aromatization in mitochondria isolated from human ovaries and placentae. A given quantity of the antibody produces the same percent inhibition of aromatization in microsomes and mitochondria of both ovaries and placentae. These data, in addition to the low specific activity observed for the mitochondrial aromatase, indicate that aromatization in mitochondria probably results from microsomal contamination.
D000735:Androstenedione / Q000378:metabolism; D001141:Aromatase / Q000378:metabolism*; D005260:Female; D006801:Humans; D008861:Microsomes / Q000201:enzymology; D008928:Mitochondria / Q000201:enzymology; D009251:NADPH-Ferrihemoprotein Reductase; D010053:Ovary / Q000201:enzymology*; D010088:Oxidoreductases / Q000378:metabolism*; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy
D000735:Androstenedione; D010088:Oxidoreductases; D001141:Aromatase; D009251:NADPH-Ferrihemoprotein Reductase