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  • 1
    Electronic Resource
    Electronic Resource
    Purification, crystallization and preliminary X-ray crystallographic analysis of lactoperoxidase from buffalo milk (1995)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 51 (1995), S. 1094-1096 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The lactoperoxidase was prepared from buffalo milk and purified using CM-Sephadex C-50 and Sephadex G-100. The activity of the enzyme was measured using 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) diammonium salt as a chromogenic substrate at pH 6.0. The purified protein was crystallized from 0.01 M sodium phosphate buffer (pH 8.0) with 10%(v/v) ethanol by the sitting-drop vapour-diffusion method. The green-coloured plate-like crystals are orthorhombic in space group P212121 with unit-cell dimensions a = 116.9, b = 103.2 and c = 62.3 Å. The asymmetric unit contains one molecule with a solvent content of 52%. The crystals were stable in the X-ray beam and diffract beyond 3.2 Å. The native data to 3.5 Å have been collected and the structure determination is in progress.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444995004422
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  • 2
    Electronic Resource
    Electronic Resource
    Subtilisin BPN' at 1.6 Å Resolution: Analysis for Discrete Disorder and Comparison of Crystal Forms (1996)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 52 (1996), S. 1125-1135 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: The three-dimensional structure of the serine protease subtilisin BPN′ (SBT) has been refined at 1.6 Å resolution in space group C2 to a final R value of 0.17. 17 regions of discrete disorder have been identified and analyzed. Two of these are dual-conformation peptide units; the remainder involve alternate rotamers of side chains either alone or in small clusters. The structure is compared with previously reported high-resolution models of SBT in two other space groups, P212121 and P21. Apart from the surface, there are no significant variations in structure among the three crystal forms. Structural variations observed at the protein surface occur predominantly in regions of protein–protein contact. The crystal packing arrangements in the three space groups are compared.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0907444996007500
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Modulation of phospholipase A2 activity generated by molecular evolution (1999)
    Springer
    Cellular and molecular life sciences 56 (1999), S. 384-397 
    Details
    ISSN: 1420-9071
    Keywords: Key words. Phospholipase A2; molecular evolution;inhibitor; pharmacological sites; enzyme activity; enzyme toxicity.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Snake venom oligomeric neurotoxins offer several unique examples of modulation of phospholipase A2 (PLA2) activity generated by molecular evolution. This phenomenon was found in evolutionary younger snakes and is probably common for representatives of the genus Vipera. At present, the best-studied example is the heterodimeric neurotoxin vipoxin from the venom of the southeast European snake Vipera ammodytes meridionalis. It is a complex between a basic strongly toxic PLA2 and an acidic and catalytically inactive PLA2-like component (Inh). This is the first reported example of a high degree of structural homology (62%) between an enzyme and its natural protein inhibitor. The inhibitor is a product of the divergent evolution of the unstable PLA2 in order to stabilize it and to preserve the pharmacological activity/toxicity for a long time. Inh reduces both the catalytic activity and toxicity of PLA2. Vipoxin also illustrates evolution of the catalytic into a inhibitory function. Vipoxin analogues have been found in the venom of viperid snakes inhabiting diverse regions of the world. An attempt is made to explain modulation of the toxic function by the three-dimensional structure of vipoxin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s000180050440
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    Paper (German National Licenses)
    Fulltext
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