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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Current genetics 29 (1996), S. 437-440 
    ISSN: 1432-0983
    Keywords: Key words Yeast ; Formaldehyde ; Hyper-resistance ; Alcohol dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  In an attempt to clone genes involved in resistance to formaldehyde we have screened a genomic library based on the episomal plasmid YEp24 for the ability to increase resistance to formaldehyde in a wild-type strain. In addition to SFA, the gene encoding the formaldehyde dehydrogenase Adh5, an enzyme most potent in formaldehyde de-toxification, we isolated a second plasmid that conferred a less pronounced but significant hyper-resistance to formaldehyde. Its passenger DNA contained the gene ADH1, encoding alcohol dehydrogenase 1 (EC 1.1.1.1), which could be shown to be responsible for the observed hyper-resistance phenotype. Construction of an adh1-0 mutant revealed that yeast lacking a functional ADH1 gene is sensitive to formaldehyde. While glutathione is essential for Adh5-mediated formaldehyde de-toxification, Adh1 reduced formaldehyde best in the absence of this thiol compound. Evidence is presented that formaldehyde is a substrate for Adh1 in vivo and in vitro and that its cellular de-toxification employs a reductive step that may yield methanol.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Current genetics 29 (1996), S. 437-440 
    ISSN: 1432-0983
    Keywords: Yeast ; Formaldehyde ; Hyper-resistance ; Alcohol dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In an attempt to clone genes involved in resistance to formaldehyde we have screened a genomic library based on the episomal plasmid YEp24 for the ability to increase resistance to formaldehyde in a wild-type strain. In addition toSFA, the gene encoding the formaldehyde dehydrogenase Adh5, an enzyme most potent in formaldehyde de-toxification, we isolated a second plasmid that conferred a less pronounced but significant hyper-resistance to formaldehyde. Its passenger DNA contained the geneADH1, encoding alcohol dehydrogenase 1 (EC 1.1.1.1), which could be shown to be responsible for the observed hyper-resistance phenotype. Construction of anadh1-0 mutant revealed that yeast lacking a functionalADH1 gene is sensitive to formaldehyde. While glutathione is essential for Adh5-mediated formaldehyde de-toxification, Adh1 reduced formaldehyde best in the absence of this thiol compound. Evidence is presented that formaldehyde is a substrate for Adh1 in vivo and in vitro and that its cellular de-toxification employs a reductive step that may yield methanol.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 3
    ISSN: 0009-2940
    Keywords: Magnesium tetrahydridoaluminate ; Magnesium halide tetrahydridoaluminate ; (Organyloxo)magnesium tetrahydridoaluminates ; X-ray structures ; Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The molecular structures of XMg(A1H4) · 4 THF (1a, 2, 3a) (X = A1H4, Cl, Br) have been determined by X-ray structural analysis. Each compound possesses a hexacoordinated Mg center and AlH4- groups bound to this center via a single hydride bridge bond. Attempts to prepare ROMg(AlH4) compounds were successful only for sterically demanding groups R (R = CMe3, CPh3, naph, mes, smes). The 2-naphthoxy derivative 7, a compound with the composition (naphO)Mg-(AlH4) · 2.5 THF, is a dimer with a central Mg2O2 ring. One of its two AlH4- groups is terminally bound to one Mg atom, the other bridges the two Mg centers. This structure indicates how AlH4- transfer may occur from ROMg(AlH4) compounds to form Mg(OR)2 and Mg(AlH4)2.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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