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  • 1
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Treatment of the wild-type strain HY 0 of Streptomyces hydrogenans with estradiol, a specific inducer of 3β,17β-hydroxysteroid dehydrogenase (17β-HSD) formation, caused several soluble proteins to bind to DNA-cellulose with altered affinity. Hydrocortisone which induces biosynthesis of 3α,20β-hydroxysteroid dehydrogenase (20β-HSD), and progesterone which induces production of both 17β- and 20β-HSD, had no effect on DNA-binding properties of the proteins. In mutants with altered activity/inducibility of 17β- and 20β-HSD only one DNA-binding protein (protein 23) still showed an altered DNA affinity in response to estradiol-treatment and this in only one strain. In other mutants the DNA affinity was not altered during induction with estradiol but the DNA affinity of protein 23 varied between low, low-and-high, and high affinity, depending on the strain. In the mutant where DNA affinity was altered by estradiol treatment the change was opposite to that found in the wild type.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 49 (1988), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Wild-type cells of Streptomyces hydrogenans ATCC 19631, strain HY A1, show a remarkable degree of genetic instability with regard to the biosynthesis of 17β-hydroxysteroid dehydrogenase. As plasmids might be responsible for this phenomenon we tried to detect plasmids in lysates of this microorganism. Streptomyces lividans, strain TK64 (pIJ916), was used as reference strain, containing a 19-kb plasmid with low abundancy. Whereas plasmid DNA could be shown in lysates of S. lividans TK64, no plasmid DNA was detectable in lysates of S. hydrogenans.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 56 (1988), S. 0 
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A procedure is described for the production of monoclonal antibodies (mAbs) against 3α,20β-hydroxysteroid dehydrogenase (3α,20β-HSD) from the actinomycete Streptomyces hydrogenans ATCC 19631. Clones which were obtained after fusion of immune cells were screened by solid-phase ELISA and immunoblotting. About 5.2% of the clones secreted immunoglobulins with specificity for 3α,20β-HSD. The purified mAbs were found to belong to subclass IgG1 and to recognize both the native enzyme as well as its identical subunits which were obtained by SDS denaturation. However, the activity of the tetrameric holoenzyme was only weakly diminished in the presence of these mAbs.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-072X
    Keywords: Enzyme induction ; Steroid transformation ; Mutagenesis ; Aerial mycelial formation ; Arginine auxotrophy ; Streptomyces hydrogenans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The effect of estradiol, hydrocortisone and progesterone on 3α,20β-and 3β,17β-hydroxysteroid dehydrogenase (HSD) in mutants of Streptomyces hydrogenans was compared to the steroid response of the wild type. Mutants were defective in arginine biosynthesis and/or aerial mycelial formation and lacked both enzymes or only 17β-HSD. Some 17β-HSD mutants had lost the ability to be induced by estradiol, by progesterone or by both. Some 20β-HSD mutants had lost the ability to be induced by hydrocortisone, by progesterone or by both. Non-inducibility of 17β-and 20β-HSD by progesterone was not co-ordinate. An additional study of the growth phase-dependent enzyme activity of the wild type after induction with estradiol, hydrocortisone and progesterone was performed.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 73 (1961), S. 65-65 
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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