JBC Avanti Polar Lipids

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Human Placental 17ß-Estradiol Dehydrogenase

III. THE SEPARATION OF A 17{beta}-ESTRADIOL-DEPENDENT TRANSHYDROGENASE

Harry J. Karavolas 1 and Lewis L. Engel 1

From the 1 From the John Collins Warren Laboratories of the Huntington Memorial Hospital of Harvard University at the Massachusetts General Hospital, and the Department of Biological Chemistry, Harvard Medical School, Boston, Massachusetts 02114

Two placental enzyme systems that catalyze the transfer of hydrogen from reduced triphosphopyridine nucleotide to diphosphopyridine nucleotide in the presence of 17ß-estradiol have been separated by chromatography on hydroxyapatite. One effects a substrate (17ß-estradiol)-mediated transhydrogenation in the presence of DPN- and TPN-linked 17ß-estradiol dehydrogenase activities and is completely inhibited by 1.67 M NaCl. The other is a 17ß-estradiol-dependent transhydrogenase unassociated with 17ß-estradiol dehydrogenase activities; its activity is increased 2.5 times in the presence of 1.67 M NaCl.

Submitted on April 6, 1966


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