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  • 1
    Online Resource
    Online Resource
    Decontamination of warfare agents : enzymatic methods for the removal of B/C weapons (2008)
    Weinheim :Wiley-VCH ;
    Details
    UID:
    almafu_9959327858902883
    Format: 1 online resource (xviii, 293 pages) : , illustrations, 1 map
    ISBN: 9783527621620 , 3527621628 , 9783527621637 , 3527621636
    Content: Based on results previously restricted for military use and inaccessible to the public, this practice-oriented handbook introduces the use of enzymes for fast and efficient decontamination of B/C weapons in various scenarios, including terrorist attacks. It draws on the internationally recognized technological leadership of the German armed forces, whose anti-B/C technology is among the most advanced worldwide. The text is rounded off with a look at future perspectives.
    Note: Decontamination of Warfare Agents; Foreword; Contents; Preface; List of Contributors; 1 The History of Biological Warfare; 2 History of Chemical Warfare; 3 Monitoring and New Threats of Chemical/Biological Weapons; 4 Biological Warfare Agents; 5 Chemical Warfare Agents; 6 Decontamination of Biological Warfare Agents; 7 Decontamination of Chemical Warfare Agents; 8 A Short Introduction to Enzyme Catalysis; 9 Hydrolytic Enzymes for Chemical Warfare Agent Decontamination; 10 Laccases Oxidative Enzymes for Bioremediation of Xenotics and Inactivation of Bacillus Spores. , 11 Medical Aspects of Chemical Warfare Agents12 Microemulsions: A Versatile Carrier for Decontamination Agents; 13 Immobilization of Enzymes; 14 Road Ahead; Index.
    Additional Edition: Print version: Decontamination of warfare agents. Weinheim : Wiley-VCH ; [Chichester] : [John Wiley, distributor], ©2008 ISBN 9783527317561
    Additional Edition: ISBN 3527317562
    Language: English
    Keywords: Electronic books. ; Electronic books. ; Electronic books.
    DOI: 10.1002/9783527621620
    URL: https://onlinelibrary.wiley.com/doi/book/10.1002/9783527621620
    URL: https://onlinelibrary.wiley.com/doi/book/10.1002/9783527621620
    URL: https://onlinelibrary.wiley.com/doi/book/10.1002/9783527621620
    Library Location Call Number Volume/Issue/Year Availability
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    Online Resource
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    HU Berlin
    FU Berlin
  • 2
    Online Resource
    Online Resource
    Adduct of the blistering warfare agent sesquimustard with human serum albumin and its mass spectrometric identification for biomedical verification of exposure (2020)
    Berlin : Humboldt-Universität zu Berlin
    Details
    UID:
    edochu_18452_27238
    Format: 1 Online-Ressource (15 Seiten)
    ISSN: 1618-2642 , 1618-2642
    Content: Apart from the well-known sulfur mustard (SM), additional sulfur-containing blistering chemical warfare agents exist. Sesquimustard (Q) is one of them and five times more blistering than SM. It is a common impurity in mustard mixtures and regularly found in old munitions but can also be used in pure form. Compared to the extensive literature on SM, very little experimental data is available on Q and no protein biomarkers of exposure have been reported. We herein report for the first time the adduct of Q with the nucleophilic Cys34 residue of human serum albumin (HSA) formed in vitro and introduce two novel bioanalytical procedures for detection. After proteolysis of this HSA adduct catalyzed either by pronase or by proteinase K, two biomarkers were identified by high-resolution tandem mass spectrometry (MS/HR MS), namely a dipeptide and a tripeptide, both alkylated at their Cys residue, which we refer to as HETETE-CP and HETETE-CPF. HETETE represents the Q-derived thio-alkyl moiety bearing a terminal hydroxyl group: “hydroxyethylthioethylthioethyl.” Targeting both peptide markers from plasma, a micro liquid chromatography–electrospray ionization tandem mass spectrometry method working in the selected reaction monitoring mode (μLC-ESI MS/MS SRM) was developed and validated as well suited for the verification of exposure to Q. Fulfilling the quality criteria defined by the Organisation for the Prohibition of Chemical Weapons, the novel methods enable the detection of exposure to Q alone or in mixtures with SM. We further report on the relative reactivity of Q compared to SM. Based on experiments making use of partially deuterated Q as the alkylating agent, we rule out a major role for six-membered ring sulfonium ions as relevant reactive species in the alkylation of Cys34. Furthermore, the results of molecular dynamics simulations are indicative that the protein environment around Cys34 allows adduct formation with elongated but not bulky molecules such as Q, and identify important hydrogen bonding interactions and hydrophobic contacts. Graphical abstract
    Content: Peer Reviewed
    In: Heidelberg : Springer, 412,28, Seiten 7723-7737, 1618-2642
    Language: English
    DOI: 10.1007/s00216-020-02917-w
    DOI: 10.18452/26539
    URN: urn:nbn:de:kobv:11-110-18452/27238-4
    URL: Volltext  (kostenfrei)
    Library Location Call Number Volume/Issue/Year Availability
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    Online Resource
    Fulltext
    HU Berlin
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