Unique rearrangement of ergocalciferol side chain in vitro: production of a biologically highly active homologue of 1,25-dihydroxyvitamin D3

Biochemistry ◽  
1986 ◽  
Vol 25 (19) ◽  
pp. 5512-5518 ◽  
Author(s):  
Yoko Tanaka ◽  
Rafal R. Sicinski ◽  
Hector F. DeLuca ◽  
Hiroshi Sai ◽  
Nobuo Ikekawa
Keyword(s):  
Side Chain ◽  
In Vitro Production ◽  
Dihydroxyvitamin D3 ◽  
1,25 Dihydroxyvitamin D3 ◽  
Highly Active ◽  
Vitro Production

IN VITRO PRODUCTION OF TESTOSTERONE AND ANDROST-4-ENE-3,17-DIONE IN A HUMAN OVARIAN HOMOGENATE

1961 ◽  
Vol 37 (1) ◽  
pp. 19-23 ◽  
Author(s):  
N. Kase ◽  
E. Forchielli ◽  
R. I. Dorfman
Keyword(s):  
Isotope Dilution ◽  
In Vitro Production ◽  
Highly Active ◽  
Normal Human ◽  
Vitro Production

ABSTRACT Testosterone and androst-4-ene-3,17-dione have been isolated and identified by isotope dilution techniques from an incubation of 7-3H-progesterone and 14C-17α-hydroxyprogesterone with a normal human ovarian homegenate. This offers substantial proof that the production of this highly active androgen is possible under normal physiological circumstances.

scholarly journals Heterologous Expression, Purification, and Characterization of a Highly Active Xylose Reductase from Neurospora crassa

2005 ◽  
Vol 71 (3) ◽  
pp. 1642-1647 ◽  
Author(s):  
Ryan Woodyer ◽  
Michael Simurdiak ◽  
Wilfred A. van der Donk ◽  
Huimin Zhao
Keyword(s):  
Neurospora Crassa ◽  
Xylose Reductase ◽  
Whole Genome Sequence ◽  
High Yield ◽  
In Vitro Production ◽  
Purification And Characterization ◽  
Highly Active ◽  
Vitro Production

ABSTRACT A xylose reductase (XR) gene was identified from the Neurospora crassa whole-genome sequence, expressed heterologously in Escherichia coli, and purified as a His6-tagged fusion in high yield. This enzyme is one of the most active XRs thus far characterized and may be used for the in vitro production of xylitol.

The psychrotrophic yeast Sporobolomyces roseus LOCK 1119 as a source of a highly active aspartic protease for the in vitro production of antioxidant peptides

2018 ◽  
Vol 65 (5) ◽  
pp. 726-738 ◽  
Author(s):  
Aneta M. Białkowska ◽  
Joanna Krysiak ◽  
Tomasz Florczak ◽  
Katarzyna M. Szulczewska ◽  
Marta Wanarska ◽  
...  
Keyword(s):  
Aspartic Protease ◽  
Antioxidant Peptides ◽  
In Vitro Production ◽  
Highly Active ◽  
Sporobolomyces Roseus ◽  
Vitro Production

THE IN VITRO PRODUCTION OF ANDROGENS BY FOLLICULAR TISSUE OF RABBITS

1964 ◽  
Vol 47 (2) ◽  
pp. 306-313 ◽  
Author(s):  
Denis Gospodarowicz
Keyword(s):  
In Vitro Production ◽  
Vitro Production

ABSTRACT Incubation in vitro of rabbit follicles in separate experiments with dehydroepiandrosterone-14C (DHEA-14C), progesterone-14C and pregnenolone-3H in the presence of FSH gave the following results: 39 % of the radioactivity of DHEA-14C is converted to androstenedione and testosterone, while only 3 % of the radioactivity of either progesterone-14C or pregnenolone-3H is found in the androgen fraction. From the ratio of testosterone to androstenedione formed from the three precursors, the results are interpreted to mean that DHEA and pregnenolone, and not progesterone, are precursors of androgens in the follicle.

Oxygenation of 18-hydroxycorticosterone as the final reaction for aldosterone biosynthesis

1984 ◽  
Vol 107 (3) ◽  
pp. 395-400 ◽  
Author(s):  
Itaru Kojima ◽  
Etsuro Ogata ◽  
Hiroshi Inano ◽  
Bun-ichi Tamaoki
Keyword(s):  
Carbon Monoxide ◽  
Hydroxysteroid Dehydrogenase ◽  
Dependent Manner ◽  
In Vitro Production ◽  
Mitochondrial Preparation ◽  
Final Reaction ◽  
Vitro Production ◽  
Dose Dependent ◽  
Cytochrome P 450

Abstract. Incubation of 18-hydroxycorticosterone with the sonicated mitochondrial preparation of bovine adrenal glomerulosa tissue leads to the production of aldosterone, as measured by radioimmunoassay. The in vitro production of aldosterone from 18-hydroxycorticosterone requires both molecular oxygen and NADPH, and is inhibited by carbon monoxide. Cytochrome P-450 inhibitors such as metyrapone, SU 8000. SU 10603, SKF 525A, amphenone B and spironolactone decrease the biosynthesis of aldosterone from 18-hydroxycorticosterone. These results support the conclusion that the final reaction in aldosterone synthesis from 18-hydroxycorticosterone is catalyzed by an oxygenase, but not by 18-hydroxysteroid dehydrogenase. By the same preparation, the production of [3H]aldosterone but not [3H]18-hydroxycorticosterone from [1,2-3H ]corticosterone is decreased in a dose-dependent manner by addition of non-radioactive 18-hydroxycorticosterone.

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