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Homogeneous 3 alpha-hydroxysteroid dehydrogenase (3 alpha-HSD) from rat liver cytosol displays 9, 11, and 15-hydroxyprostaglandin dehydrogenase activity. Using [14C]-PGF2 alpha as substrate the products of this reaction were separated by TLC and identified by autoradiography as PGE2 and PGB2. The purified enzyme catalyzes this reaction at a rate 200 times faster than cytosol. This corresponds to the rate enhancement observed when the enzyme is purified from cytosol using androsterone (a 3 alpha-hydroxysteroid) as substrate and suggests that it may represent a major 9-hydroxyprostaglandin dehydrogenase in this tissue. Although the 3 alpha-HSD has many properties in common with the 9-hydroxyprostaglandin dehydrogenase of rat kidney, rat kidney contains no protein that is immunodetectable with polyclonal antibody raised against the purified 3 alpha-HSD.
T M Penning, and
R B Sharp
February 1992,
The Journal of steroid biochemistry and molecular biology,
T M Penning, and
R B Sharp
April 1994,
Steroids,
T M Penning, and
R B Sharp
July 1992,
Biochemical pharmacology,
T M Penning, and
R B Sharp
November 1989,
Journal of biochemistry,
T M Penning, and
R B Sharp
July 1998,
Biochemistry,
T M Penning, and
R B Sharp
June 1991,
Molecular endocrinology (Baltimore, Md.),
T M Penning, and
R B Sharp
March 1990,
The Biochemical journal,
T M Penning, and
R B Sharp
December 1976,
Biochemical pharmacology,
T M Penning, and
R B Sharp
March 1992,
Biochemical pharmacology,
T M Penning, and
R B Sharp
May 1991,
Journal of biochemistry,
