Linked Life Data

237755

Source:http://linkedlifedata.com/resource/pubmed/id/237755

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1975-10-7
pubmed:abstractText
The 17 beta-hydroxysteroid dehydrogenase which was purified from porcine testicular microsomal fraction [Inano, H. and Tamaoki, B (1974) Eur. J. Biochem. 44, 13-23] catalyzed the reduction of androstenedione to testosterone with the accompanying oxidation of equimolar NADPH. For the oxido-reduction of the steroids, the 17 beta-hydroxysteroid dehydrogenase preferred NADP(H) to NAD(h). Transhydrogenation from NADPH to NAD+ or NADH to NADP+ through the cyclic oxido-reduction of the steroids by the purified 17 beta hydroxysteroid dehydrogenase preparation was not spectrophotometrically detectable, because of selective preference of the testicular 17 beta-hydroxysteroid dehydrogenase against NADP(H). To examine stereospecific transfer of the hydrogen from NADPH to androstenedione by the purified 17 beta-hydroxysteroid dehydrogenase, the following tritiated cofactors were synthesized: [4-3-H]NADP+ was prepared by catalytic replacement from non-radioactive NADP+ and 3H2O in the presence of potassium cyanide. Then, [4-pro-R3H]NADPH was enzymatically synthesized from the [4-3H]NADP+ by glucose 6-phosphate and its dehydrogenase. On the other hand, [4-pro-S-3H]NADPH was prepared from the [4-3H]NADP+ by isocitrate and isocitrate dehydrogenase. When androstenedione was incubated with the 17 beta-hydroxysteroid dehydrogenase in the presence of these stereospecifically 3H-labeled cofactors, only the tritium located at 4-pro-S position of the nicotinamide moiety of NADPH was transferred to testosterone. The location of the tritium in the testosterone molecule produced, 17alpha-position of the steroid, was assigned by the fact that the tritium of the testosterone remained in its molecule after acetylation, but was completely lost by oxidation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
53
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
319-26
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Relationship between steroids and pyridine nucleotides in the oxido-reduction catalyzed by the 17 beta-hydroxysteroid dehydrogenase purified from the porcine testicular microsomal fraction.
pubmed:publicationType
Journal Article