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Journal ArticleDOI

Kinetic studies of rat ovarian 20α-hydroxysteroid dehydrogenase

Piamsook Pongsawasdi, +1 more
- 25 May 1984 - 
- Vol. 799, Iss: 1, pp 51-58
TLDR
Rat ovarian 20α-hydroxysteroid dehydrogenase was purified 230-fold with a 48% recovery through a 3-step process involving hydrophobic, gel filtration and gree dye affinity chromatography, indicating a sequential mechanism for the enzyme.
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This article is published in Biochimica et Biophysica Acta.The article was published on 1984-05-25. It has received 14 citations till now. The article focuses on the topics: Product inhibition & Non-competitive inhibition.

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Citations
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Journal ArticleDOI

The kinetic mechanism catalysed by homogeneous rat liver 3 alpha-hydroxysteroid dehydrogenase. Evidence for binary and ternary dead-end complexes containing non-steroidal anti-inflammatory drugs.

TL;DR: Rat liver 3 alpha-hydroxysteroid dehydrogenase (3 alpha-HSD) is an NAD(P)(+)-dependent oxidoreductase that is potently inhibited at its active site by non-steroidal anti-inflammatory drugs (NSAIDs).
Journal ArticleDOI

Conversion of mammalian 3alpha-hydroxysteroid dehydrogenase to 20alpha-hydroxysteroid dehydrogenase using loop chimeras: changing specificity from androgens to progestins.

TL;DR: This study represents an example where sex hormone specificity can be changed at the enzyme level with a resultant shift in k(cat)/K(m) for the desired reaction of 2 x 10(11).
Journal ArticleDOI

Expression, Purification and Characterization of the Rat Luteal 20α-Hydroxysteroid Dehydrogenase1

TL;DR: To investigate whether phosphorylation and/or glycosylation affect the activity of 20αHSD and to study its kinetic and biochemical properties, both bacterial and insect expression systems are established for obtaining large quantities of enzyme.
Journal ArticleDOI

Purification and characterization of a novel form of 20 alpha-hydroxysteroid dehydrogenase from Clostridium scindens.

TL;DR: Results indicate that this enzyme is a novel form of 20 alpha-hydroxysteroid dehydrogenase, which was highly specific for adrenocorticosteroid substrates possessing 17 alpha, 21-dihydroxy groups.
Journal ArticleDOI

Purification and characterization of rat ovarian 20α-hydroxysteroid dehydrogenase

TL;DR: Two types of 20 alpha-HSD with very similar molecular structures are present in the rat ovary, indicating that the enzyme fractions were single-stranded, monomeric polypeptides.
References
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Journal ArticleDOI

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

TL;DR: This assay is very reproducible and rapid with the dye binding process virtually complete in approximately 2 min with good color stability for 1 hr with little or no interference from cations such as sodium or potassium nor from carbohydrates such as sucrose.
Journal ArticleDOI

The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis

TL;DR: The results show that the polyacrylamide gel electrophoresis method can be used with great confidence to determine the molecular weights of polypeptide chains for a wide variety of proteins.
Journal Article

Regulation of T cell differentiation: in vitro induction of 20 alpha-hydroxysteroid dehydrogenase in splenic lymphocytes from athymic mice by a unique lymphokine.

TL;DR: In vivo, the expression of 20 alpha SDH is thymus dependent, in that splenic lymphocytes from athymic mice have only low levels of activity, although the levels of enzyme activity increase gradually with age, and induction is blocked by mitomycin C, suggesting a requirement for cell proliferation.
Journal ArticleDOI

Progesterone Catabolism in the Rat Ovary: A Regulatory Mechanism for Progestational Potency During Pregnancy

TL;DR: Changes in rat ovarian 20α-OH-SDH3 and G-6-PDH activities as well as their intraglandular distribution during pregnancy, at parturition and during lactation have been determined concurrently with measurements of the peripheral blood and uterine tissue levels of progesterone and 20 α- OH-P.
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