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  • Genetics  (1)
  • Organic Chemistry  (1)
  • Wiley-Blackwell  (2)
  • Blackwell Publishing Ltd
  • 1
    Electronic Resource
    Electronic Resource
    Sur la constitution de l'acide chondroïtine-sulfurique (1953)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 36 (1953), S. 597-605 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Reprenant l'etude de la constitution de l'acide chondroïtine-sulfurique, nous avons pu établir: 1° Que la liaison chondrosaminique se trouve bien en C1-C4, conformément aux conclusions de Wolfrom.2° Que la liaison glucuronique se trouve en C1-C6 et non pas C1-C3.3° Que le groupe sulfate est situé en C3 ou C4 de la chondrosamine.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19530360310
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of an active GST-human Cdc2 fusion protein kinase expressed in the fission yeast Schizosaccharomyces pombe: A new approach to the study of cell cycle control proteins (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 1631-1638 
    Details
    ISSN: 0749-503X
    Keywords: Schizosaccharomyces pombe ; cell cycle ; Cdc2 kinase ; GST ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Characterization of cdk (cyclin dependent kinases) substrates and studies of their regulation require purified enzymatic complexes of cdc2-related catalytic and cyclin regulatory subunits. We produced human Cdc2 kinase in the fission yeast Schizosaccharomyces pombe as a fusion protein with glutathione S-transferase (GST). The GST-human Cdc2p fusion protein was active in vivo since it rescued a temperature-sensitive allele of cdc2. The fusion protein was purified using a one-step chromatography procedure with glutathione-Sepharose and exhibited a catalytic activity in vitro. Yeast cyclin B and suc1 were found in association with GST-Cdc2. A 17-fold stimulation of GST-Cdc2 kinase activity was obtained by incubation of recombinant human cyclin A with the S. pombe cellular extract prior to affinity purification. This indicates that cyclin concentration is limiting in this overexpression system. These findings describe a fast and easy production of active recombinant human Cdc2 kinase in yeast that can be used for biochemical studies.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320101212
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