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  • 2000-2004  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Preliminary X-ray diffraction studies of the external functional unit RtH2-e from the Rapana thomasiana (2001)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 1663-1665 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The `external' oxygenated functional unit RtH2-e of the Rapana hemocyanin subunit RHSS2 was isolated and crystallized. X-ray intensity data to 3.3 Å resolution have been collected at 100 K and the structure has been solved using the molecular-replacement method. The space group is assigned to be the tetragonal P43212, with unit-cell parameters a = b = 105.5, c = 375.0 Å.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444901012124
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Identification of Small Peptides Generated in Spanish Dry-cured Ham (2003)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 68 (2003), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: : A water-soluble extract of dry-cured ham was fractionated by gel filtration chromatography. Collected fractions (below 1200 Da) were sensory-analyzed and subjected to amino acid analysis with and without previous acid hydrolysis, in order to determine the amino acid and peptide distribution. Those fractions with the highest peptide amount were further separated by reverse-phase and cation-exchange high-performance liquid chromatography in order to isolate the peptides and sequence them. The results demonstrated the presence of small peptides, mainly dipeptides. The combination of these peptides and free amino acids may contribute to the characteristic taste in the savory fractions of dry-cured ham.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2003.tb14115.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Identification of Macrophage Migration Inhibitory Factor Isoforms in Bovine Brain (2000)
    Springer
    Neurochemical research 25 (2000), S. 1125-1129 
    Details
    ISSN: 1573-6903
    Keywords: Macrophage migration inhibitory factor ; isoforms ; primary structure ; bovine brain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract In the course of the study of the primary structures and molecular mechanisms of action of immunologically active compounds of the nervous system we have isolated from the soluble fraction of total bovine brain two heat-stable proteins. The purification procedure was mainly based on DEAE-Servacel ion-exchange chromatography and reversed-phase HPLC. The proteins were identified by the N-terminal Edman microsequence analysis and database searching as macrophage migration inhibitory factor (MIF). The N-terminal sequences for MIF1 and MIF2 were found to be identical. According to mass spectral analysis, the molecular masses for MIF1 and MIF2 were determined respectively as 12,369.21 and 12,299.7 Da. In addition, we have also isolated a third peptide having the same N-terminal sequence and Mr 9,496.2 that seems to be a proteolytic fragment of MIF. Using p-hydroxyphenylpyruvate as a substrate, we have not revealed tautomerase activity of either MIF1 or MIF2. As both the immunologic and enzymatic activities were reported to be expressed by the oligomeric structure of MIF, we suggest that the present study may give additional information on MIF in terms of structural properties of this protein. A comparatively simple purification procedure is presented that may be widely used for simultaneous isolation in one run of MIF isoforms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007678214348
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    Paper (German National Licenses)
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