-transparent.png){kind=logo}
When a crude extract of Pseudomonas testosteroni induced with testosterone was subjected to polyacrylamide gel electrophoresis, six bands that stained for 17 beta-hydroxysteroid dehydrogenase activity was observed. A protein fraction containing the enzyme corresponding to the fastest migrating band and devoid of the other hydroxysteroid dehydrogenase activities has been obtained. This preparation appears to be distinct from the previously isolated 3(17) beta-hydroxysteroid dehydrogenase (EC 1.1.1.51) in its chromatography properties on DEAE-cellulose, substrate and cofactor specificity, immunological properties and heat stability. The preparation appears devoid of 3alpha-, 3beta-, 11beta-, 17alpha-, 20alpha-, and 20beta-hydroxysteroid dehydrogenase activities. The enzyme transfers th 4-pro-S-hydrogen of NADH from estradiol-17beta (1,3,5(10)estratriene-3,17beta-diol) to estrone (3-hydroxy-1,3,5(10)-estratriene-17-one).
E V Groman, and
L L Engel
May 1979,
Journal of steroid biochemistry,
E V Groman, and
L L Engel
January 1995,
Comptes rendus des seances de la Societe de biologie et de ses filiales,
E V Groman, and
L L Engel
February 1993,
The Journal of steroid biochemistry and molecular biology,
E V Groman, and
L L Engel
April 1987,
Biochemistry,
E V Groman, and
L L Engel
January 1977,
Biochimie,
E V Groman, and
L L Engel
August 1985,
FEBS letters,
E V Groman, and
L L Engel
March 1967,
The Journal of clinical endocrinology and metabolism,
E V Groman, and
L L Engel
September 1964,
Biochimica et biophysica acta,
E V Groman, and
L L Engel
July 1974,
European journal of biochemistry,
E V Groman, and
L L Engel
August 1991,
Gene,
