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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 170 (1998), S. 442-450 
    ISSN: 1432-072X
    Keywords: Key words Tissierella creatinophila ; Sarcosine ; reductase ; Protein C ; Protein A ; Protein Bsarcosine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Sarcosine reductase is the only reductase system present in Tissierella creatinophila when grown on creatinine plus formate. The acetyl-phosphate-forming component protein C was purified to homogeneity. SDS-PAGE of the purified protein revealed two protein bands with apparent mol. masses of 62 and 50 kDa. The N-terminal amino acid sequence of the two subunits was determined. Antibodies raised against each of the subunits of protein C from Eubacterium acidaminophilum cross-reacted with the corresponding protein present in T. creatinophila, Clostridium litorale and Clostridium sporogenes. The arsenate-dependent hydrolysis of acetyl phosphate catalyzed by protein C was partly inhibited by antibodies directed against the large subunit. Antibodies raised against the small subunit were twice as effective, which indicates that this subunit is the primary site of acetyl transfer from acetyl phosphate. The protein A component of the sarcosine reductase of T. creatinophila was purified to homogeneity by cochromatography with thioredoxin reductase on DEAE-Sephacel, hydroxylapatite, Q-Sepharose, and Sephacryl 100-HR. Protein A had an apparent mol. mass of 21 kDa. Its N-terminal amino acid sequence showed high similarities to that of other proteins A. Initial steps for the purification and preliminary characterization of the sarcosine-specific, substrate-binding protein Bsarcosine component of T. creatinophila indicated the involvement of a 50-kDa protein.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0009-2940
    Keywords: Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Die im Titel genannte Umlagerung wird von Substituenten im Anilinrest nur wenig beeinflußt (ρ in 97 proz. Methanol ∼ 0.9); für die Ks-Werte der Aminoxid-hydrochloride ergab sich ρ ∼ 1.3. Demnach dürften die RG-Unterschiede hauptsächlich durch Solvatationsunterschiede der Grundzustände bedingt sein. Der Substituenteneinfluß auf die Umlagerung der (hypothetischen) nicht-solvatisierten Aminoxide läßt sich zu ρ ∼-0.4 abschätzen und steht im Einklang mit einem radikalischen Dissoziations-Rekombinations-Mechanismus.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 0075-4617
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Die Umlagerungsgeschwindigkeit der N-Benzyl-N-methyl-anilinoxide 4 hängt nur wenig vom Substituenten im Benzyl-Kern ab, sehr aber vom Solvatationsvermögen des Lösungsmittels. In 97-proz. wäßrigem Methanol und in Tetrahydrofuran/Wasser beträgt ΔS≠ = 20-44 E. E. Bei der Isomerisation von 4a ließ sich ESR-spektroskopisch N-Phenyl-N-methyl-N-oxid nachweisen. Die Befunde sprechen für einen zweistufigen radikalischen Ablauf der Umlagerung. Ist c 〈 10-3 Mol/l, so vollzieht sich der Prozeß nahezu ganz intramolekular, d. h. über ein internes Radikalpaar (7). Beim optisch aktiven N-Benzyl-N-methyl-anilinoxid ist kα = kUmlagerung.
    Additional Material: 6 Tab.
    Type of Medium: Electronic Resource
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