Abstract
The activity of pyridine nucleotide-linked 17β-and 20α-hydroxysteroid dehydrogenase (s) was detected in HeLa S3 cells. Addition of progesterone to cultures failed to increase the 20α-hydroxysteroid dehydrogenase activity of the cells. The enzyme was partially purified by ammonium sulfate fractionation and chromatography on Bio-gel P-100, and the molecular weight of the enzyme was estimated at approximately 30, 000. The enzyme (s) could operate progesterone, 17α-hydroxyprogesterone (20α-hydroxysteroid dehydrogenase) and androst-4-ene-3, 17-dione (17β-hydroxysteroid dehydrogenase) in the presence of either NADH or NADPH. However, there was a small difference of elution patterns from the Bio-gel column between the NADH-and NADPHlinked enzymes, while the NADPH-linked 17β-hydroxysteroid dehydrogenase activity was eluted at the same void volume as the NADPH-linked 20α-hydroxysteroid dehydrogenase activity.
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