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  • Organic Chemistry  (3)
  • ATP-sulfurylase-adenosine 5′-phosphosulfate sulfotransferase  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Planta 179 (1989), S. 228-234 
    ISSN: 1432-2048
    Keywords: ATP-sulfurylase-adenosine 5′-phosphosulfate sulfotransferase ; Pisum (sulfate reduction) ; Proplastid ; Sulfite reductase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The localization of enzymes of assimilatory sulfate reduction was examined in roots of 5-d-old pea (Pisum sativum L.) seedlings. During an 8-h period, roots of intact plants incorporated more label from 35SO 4 2- in the nutrient solution into the amino-acid and protein fractions than shoots. Excised roots and roots of intact plants assimilated comparable amounts of radioactivity from 35SO 4 2- into the amino-acid and protein fractions during a 1-h period, demonstrating that roots of pea seedlings at this stage of development were not completely dependent on the shoots for reduced sulfur compounds. Indeed, these roots contained activities of ATP-sulfurylase (EC 2.7.7.4), adenosine 5′-phosphosulfate sulfotransferase, sulfite reductase (EC 1.8.7.1) and O-acetyl-l-serine sulfhydrylase (EC 4.2.99.8) at levels of 50, 30, 120 and 100%, respectively, of that in shoots. Most of the extractable activity of adenosine 5′-phosphosulfate sulfotransferase was detected in the first centimeter of the root tip. Using sucrose density gradients for organelle separation from this part of the root showed that almost 40% of the activity of ATP-sulfurylase, adenosine 5′-phosphosulfate sulfotransferase and sulfite reductase banded with the marker enzyme for proplastids, whereas only approximately 7% of O-acetyl-l-serine sulfhydrylase activity was detected in these fractions. Because their distributions on the gradients were very similar to that of nitrite reductase, a proplastid enzyme, it is concluded that ATP-sulfurylase, adenosine 5′-phosphosulfate sulfotransferase and sulfite reductase are also exclusively or almost exclusively localized in the proplastids of pea roots. O-Acetyl-l-serine sulfhydrylase is predominantly present in the cytoplasm.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 31 (1948), S. 1617-1623 
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Durch Reduktion mit Lithiumaluminiumhydrid wurde aus den entsprechenden Estern von α-Aminocarbonsäuren die folgenden Aminoalkohole dargestellt: D, L-Phenylalaninol, L(-)-Phenylalaninol, L(-)-Tyrosinol, L(+)-Alaninol, L(+)-Leucinol, L,(+)-2-Oxymethylpyrrolidin (L(+)-Prolinol), L(+)-2-Aminobutandiol-(1,4) (L(+)-Asparaginol), D, L-2-Aminobutandiol-(1,4) (D, L-Asparaginol) und 2-Amino-propandiol-( 1,3).
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 32 (1949), S. 1156-1157 
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Durch Reduktion mit Lithiumaluminiumhydrid wurden aus L-Valin-methylester L-Valinol und aus L-Tyrosin-methylester L-Tyrosinol in guten Ausbeuten hergestellt.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 32 (1949), S. 1936-1938 
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Durch Reduktion von Dibenzoyl-L-histidinmethylester mit LiAlH4 wurden Monobenzoyl-L-histidinol und aus letzterem durch Verseifung L-Histidinol hergestellt. Letztere Verbindung zeigt ähnliche pharmakologische Wirkung wie Histamin, aber erst in 1000-3000 mal höherer Dosis.
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