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  • Organic Chemistry  (3)
  • ATP-sulfurylase-adenosine 5′-phosphosulfate sulfotransferase  (1)
  • Albumin  (1)
  • Forests  (1)
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Years
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    BBA - Protein Structure 670 (1981), S. 424-427 
    ISSN: 0005-2795
    Keywords: Albumin ; Antibody development ; ELISA ; Immunodiffusion ; Peptide synthesis ; Proalbumin
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1939
    Keywords: Key words15N ; Forests ; Spruce ; Picea abies ; NO2 deposition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The 15N ratio of nitrogen oxides (NOx) emitted from vehicles, measured in the air adjacent to a highway in the Swiss Middle Land, was very high [δ15N(NO2) = +5.7‰]. This high 15N abundance was used to estimate long-term NO2 dry deposition into a forest ecosystem by measuring δ15N in the needles and the soil of potted and autochthonous spruce trees [Picea abies (L.) Karst] exposed to NO2 in a transect orthogonal to the highway. δ15N in the current-year needles of potted trees was 2.0‰ higher than that of the control after 4 months of exposure close to the highway, suggesting a 25% contribution to the N-nutrition of these needles. Needle fall into the pots was prevented by grids placed above the soil, while the continuous decomposition of needle litter below the autochthonous trees over previous years has increased δ15N values in the soil, resulting in parallel gradients of δ15N in soil and needles with distance from the highway. Estimates of NO2 uptake into needles obtained from the δ15N data were significantly correlated with the inputs calculated with a shoot gas exchange model based on a parameterisation widely used in deposition modelling. Therefore, we provide an indication of estimated N inputs to forest ecosystems via dry deposition of NO2 at the receptor level under field conditions.
    Type of Medium: Electronic Resource
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  • 3
    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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  • 4
    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).
    Type of Medium: Electronic Resource
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  • 5
    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.
    Type of Medium: Electronic Resource
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  • 6
    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.
    Type of Medium: Electronic Resource
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