1971
DOI: 10.1016/0024-3205(71)90309-2
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New aspect of guinea pig liver 17β-hydroxysteroid (testosterone) dehydrogenase

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Cited by 11 publications
(8 citation statements)
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“…The NADP+-dependent enzyme was partially purified [38] and was separated into two fractions by ammonium sulfate precipitation following by DEAE-cellulose chromatography [39]. One of the fractions catalyzed dehydrogenations of both testosterone and 3-hydroxyhexobarbita1, the other fraction retained only 17t9-hydroxysteroid dehydrogenase activity.…”
Section: Puritymentioning
confidence: 99%
“…The NADP+-dependent enzyme was partially purified [38] and was separated into two fractions by ammonium sulfate precipitation following by DEAE-cellulose chromatography [39]. One of the fractions catalyzed dehydrogenations of both testosterone and 3-hydroxyhexobarbita1, the other fraction retained only 17t9-hydroxysteroid dehydrogenase activity.…”
Section: Puritymentioning
confidence: 99%
“…Purification oftestosterone 17fi-dehydrogenase. The new testosterone 17fi-dehydrogenase was purified by a modification of the procedure for 3-hydroxyhexobarbital dehydrogenase (Kageura & Toki, 1975). All steps were carried out at 0-4°C and each enzyme fraction was concentrated in a Diaflo PM-10 filter (Amicon Corp., Lexington, MA, U.S.A.).…”
Section: Methodsmentioning
confidence: 99%
“…In a previous paper we demonstrated that testosterone 17fi-dehydrogenase (NADP+) (EC 1.1.1.64), obtained from guinea-pig liver cytosol, participates in the reversible oxidation of 3-hydroxyhexobarbital [5-(3'-hydroxy-1'-cyclohexen-1'-yl)-1,5-dimethylbarbituric acid], the microsomal oxygenation product ofhexobarbital (Kageura & Toki, 1971). This enzyme was subsequently purified to homogeneity as 3hydroxyhexobarbital dehydrogenase (Kageura & Toki, 1975).…”
mentioning
confidence: 99%
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