Soluble guinea pig liver TPN dependent 17β-hydroxysteroid (testosterone) dehydrogenase: Partial purification and substrate specificity

Ammonium sulfate fractionation, DEAE-cellulose and hydroxylapatite chromatography have been employed to effect 200–230 fold purification of the soluble TPN dependent 17β-hydroxysteroid (testosterone) dehydrogenase of guinea pig liver. The purified preparations also oxidize saturated C 19-3β-hydroxys...

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Bibliographic Details
Published inSteroids Vol. 1; no. 5; pp. 508 - 527
Main Authors Joshi, Sharad G., Loverne Duncan, E., Engel, Lewis L.
Format Journal Article
LanguageEnglish
Published Elsevier Inc 01.01.1963
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Summary:Ammonium sulfate fractionation, DEAE-cellulose and hydroxylapatite chromatography have been employed to effect 200–230 fold purification of the soluble TPN dependent 17β-hydroxysteroid (testosterone) dehydrogenase of guinea pig liver. The purified preparations also oxidize saturated C 19-3β-hydroxysteroids of the 5α series and saturated C 19-17β-hydroxysteroids. Studies on substrate specificity indicate that the planarity of the substrate influences the reactivity.
ISSN:0039-128X
1878-5867
DOI:10.1016/S0039-128X(63)80107-5