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5 androstene 3 17 dione

Manufactured by Steraloids
Sourced in United States

5-androstene-3,17-dione is a steroid compound that is a precursor to various hormones such as testosterone and estrogen. It is commonly used in research and laboratory settings to study steroid biosynthesis and metabolism.

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2 protocols using 5 androstene 3 17 dione

1

Comprehensive Chemical Reagent Inventory

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Chemicals were purchased as follows: Sigma-Aldrich (St. Louis, MO): 17β-estradiol (E2), cycloheximide (CHX, translation inhibitor), 4-hydroxytamoxifen (4-OHT), finasteride (5α-reductase inhibitor), miconazole (general P450 inhibitor), exemestane (aromatase inhibitor), STX64 (steroid sulfatase inhibitor), 5-fluorouracil (5-FU), doxorubicin (Dox), actinomycin D (ActD, a transcriptional inhibitor), and flutamide (a selective androgen receptor modulator (SARM)); Tocris (Ellisville, MO): Fulvestrant (ICI 182, 780), 2,3-bis(4-hydroxyphenyl)propionitrile (DPN), an ERβ-selective agonist; 4,4',4”-(4-Propyl-[1H]-pyrazole-1,3,5-triyl)trisphenol (PPT), an ERα-selective agonist; and 4-[2-Phenyl-5,7-bis(trifluoromethyl)pyrazolo[1,5-a]pyrimidin-3-yl]phenol (PHTPP, an ERβ-selective inhibitor); Steraloids (Wilton, NH): dehydroepiandrosterone (DHEA), dihydrotestosterone (DHT), DHEA 3β-sulfate (DHEA-S), 5-androstene-3α,17α-diol (ADIOL), 5-androstene-3,17-dione (ADIONE), and 5α-androstane-3β,17β-diol (3β-Adiol). The SARM bicalutamide (Casodex) was generously provided by Astra Zeneca (Macclesfield, UK).
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2

Michaelis-Menten Kinetics of Steroid Hormones

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KSI Michaelis-Menten parameters were obtained by monitoring the 5(10)-estrene-3,17-dione and 5-androstene-3,17-dione (Steraloids, Newport, RI, USA) reaction at 248 nm (extinction coefficient, 14,800 M−1 cm−1) in a PerkinElmer Lambda 25 spectrophotometer (66 (link)). Reactions were measured at 25°C in 4 mM sodium phosphate and pH 7.2 buffer with 2% dimethyl sulfoxide (DMSO; J.T.Baker, Omaha, NE, USA) added for substrate solubility. Low buffer concentrations were used to minimize the background reaction rate. Values of kcat and KM were determined by fitting the initial rates as a function of substrate concentration to the Michaelis-Menten equation. Typically, five to seven substrate concentrations, varying from 2 to 300 μM, were used for each enzyme variant. Averaged values and errors representing the SDs are given in table S2.
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