Purification and Properties of NADP‐Dependent 17β‐Hydroxysteroid Dehydrogenase Solubilized from Porcine‐Testicular Microsomal Fraction

Itoh, Hiroshi; Tamaoki, Bun-Ichi

doi:10.1111/j.1432-1033.1974.tb03453.x

Cited by 57 publications

(13 citation statements)

References 36 publications

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“…On the other hand, the predicted pig 17␤-HSD Type3 consisted of a monomeric protein of 310 amino acid residues with a molecular weight of 34,855, which agrees with the findings for purified pig testicular 17␤-HSD Type3 (M.W. : 33,200-35,500) [6,12,13]. As shown in Fig.…”

Section: Resultssupporting

confidence: 89%

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Sequence of pig 17β-hydroxysteroid dehydrogenase Type3 cDNA and its expression in mammalian cells

Ohno

Honda

Nakajima

et al. 2006

The Journal of Steroid Biochemistry and Molecular Biology

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Section: Resultssupporting

confidence: 89%

“…Type3 enzyme was first purified in an active form from pig testis and has been characterized [6]; however, the cDNA and amino acid sequences of the pig enzyme were not elucidated. To date, the cDNA sequences of Type3 enzymes have been reported in humans [7], mice [8] and rats [9].…”

Section: Introductionmentioning

confidence: 99%

Sequence of pig 17β-hydroxysteroid dehydrogenase Type3 cDNA and its expression in mammalian cells

Ohno

Honda

Nakajima

et al. 2006

The Journal of Steroid Biochemistry and Molecular Biology

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“…The characteristics and kinetic behaviour of the 170-hydroxysteroid dehydrogenase activities distributed among the various subcellular compartments are comparable to those which have been isolated from human endometrium, placenta, testes and erythrocytes (9,(14)(15)(16)(17)(18)(19). It is noteworthy that phenolic steroids are preferred as substrate, under both oxidizing and reducing conditions, which is comparable to the behaviour of the 170-hydroxysteroid dehydrogenase isolated from placenta or endometrium.…”

supporting

confidence: 54%

In Vitro Conversion of Estradiol-17β into Estrone in Normal Human Myometrium und Leiomyoma

Pollow¹,

Sinnecker²,

Boquoi³

et al. 1978

Clinical Chemistry and Laboratory Medicine

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Summary:The specific activity of 170-hydroxysteroid dehydrogenase was measured in normal human myometrium, and in leiomyoma specimens obtained from the same tumor-bearing uterus. In all cases the normal tissue showed greater conversion of estradiol-17/3 into estrone than the neoplastic tissues. In normal myometrium of fertile women, the specific enzyme activity depended on the phase of the menstrual cycle, the highest values of 170-hydroxysteroid dehydrogenase activity being found in the early secretory phase.To determine the intracellular distribution of the 17/3-hydroxysteroid dehydrogenase, purified microsomes, mitochondria, nuclei and cytosol fractions were prepared. The purity of each fraction was monitored by marker enzymes. It was found that the enzyme was mainly located in mitochondria and microsomes. Furthermore it was demonstrated that the microsomal enzyme was bound tightly to the membranes of the endoplasmic reticulum, while the mitochondrial 17j34iydroxysteroid dehydrogenase was mainly associated with the outer membranes of the organelle.Kinetic parameters (K m -values, coenzyme requirements, temperature and pH-optima) of the cytoplasmic, nuclear, mitochondrial and microsomal enzyme of normal and neoplastic tissue were compared. In vitrO'Umwandlung von Östradiol-17ß in Östron in normalem Human-Myometrium und LeiomyomenZusammenfassung: Die spezifische Aktivität der 17|8-Hydroxysteroiddehydrogenase wurde in normalem HumanMyometrium und in Gewebeproben von Leiomyomen vergleichend gemessen. Die Gewebsproben wurden aus dem gleichen Tumor-tragenden Uterus gewonnen. Normalgewebe zeigte einen größeren Umsatz von Östradiol-170 zu Östron als Tumorgewebe. In Normal-Myometrium geschlechtsreifer Frauen variierte die spezifische Enzymaktivität in Abhängigkeit vom Menstruationszyklus: die höchsten Werte wurden in der frühen Sekretionsphase beobachtet.Um die intrazellulare Verteilung der 17|8-Hydroxysteroiddehydrogenase-Aktivität zu untersuchen, wurden hochgereinigte Mikrosomen, Mitochpndrien, Kerne und Cytoplasma präpariert. Der Reinheitsgrad der Fraktion wurde durch Leitenzyme charakterisiert. Die höchsten spezifischen Enzymaktivitäten wurden in Mitochondrien und Mikrosomen lokalisiert. Darüberhinaus wurde beobachtet, daß das mikrosomale Enzym fest mit der Membran des endoplasmatischen Retikulums verbunden ist, während die mitochondriale 17j3-Hydroxysteroiddehydrogenase mit der äußeren Membran der Mitochondrien assoziiert ist.Kinetische Parameter (K m -Werte, Coenzym-Abhängigkeit, Temperatur-und pH-Optima) des cytoplasmatischen, nuklearen, mitochondrialen und mikrosonialen Enzyms aus normalem und neoplastischem Gewebe wurden vergleichend untersucht.

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“…In the oxidation direction the same amino acid may function as a general base. The stereochemistry of hydride transfer has been elucidated for a number of HSDs using stereospecifically labeled 4-pro(R)-or 4-pro(S)-NAD(P)H (172,(181)(182)(183)(184). As an example, the reaction catalyzed by 3␣-HSD is shown in Fig.…”

Section: B Catalytic Mechanism Of Hsdsmentioning

confidence: 99%

Molecular Endocrinology of Hydroxysteroid Dehydrogenases*

1997

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Purification and Properties of NADP‐Dependent 17β‐Hydroxysteroid Dehydrogenase Solubilized from Porcine‐Testicular Microsomal Fraction

Abstract: 1.09.Reverse Reaction. !By using a partially purified enzyme preparation (40 -75 O i 0 ammonium sulfate precipitate fraction), the reaction was found to be reversible at pH 7.0 with testosterone and NADPf, Eur. J. Biochem. 44 (1974)

Cited by 57 publications

References 36 publications

Sequence of pig 17β-hydroxysteroid dehydrogenase Type3 cDNA and its expression in mammalian cells

Sequence of pig 17β-hydroxysteroid dehydrogenase Type3 cDNA and its expression in mammalian cells

In Vitro Conversion of Estradiol-17β into Estrone in Normal Human Myometrium und Leiomyoma

Molecular Endocrinology of Hydroxysteroid Dehydrogenases*

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