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  • 1
    Electronic Resource
    Electronic Resource
    The toxicological properties of impurities in malathion (1978)
    Springer
    Archives of toxicology 42 (1978), S. 95-106 
    Details
    ISSN: 1432-0738
    Keywords: Malathion ; Isomalathion ; Trimethyl phosphorothioates ; Acetylcholinesterase ; Carboxylesterase ; Potentiation of toxicity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract During a malaria eradication programme in Pakistan in 1976, out of 7,500 spraymen, 2,800 became poisoned and 5 died. The major determinant of this poisoning has been identified as isomalathion present as an impurity in the malathion. It seems almost certain that the isomalathion was produced during storage of the formulated malathion. The quantitative correlation found between isomalathion content and toxicity of many field samples of malathion has been confirmed by an examination of mixtures of pure compounds. Addition of known amounts of isomalathion to technical malathion indicates that other active substances are present. These impurities have been identified (trimethyl phosphorothioates) and have been shown to behave like isomalathion in potentiating the toxicity of malathion. Some preliminary work on their toxicological properties is reported. The mechanisms involved in the potentiation of the toxicity of malathion are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00316489
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Ferrochelatase activity inAzospirillum brasilense with reference to the influence of metal cations (1989)
    Springer
    BioMetals 2 (1989), S. 31-35 
    Details
    ISSN: 1572-8773
    Keywords: Heme synthesis ; Iron metabolism ; Membranes ; Cation inhibition ; Metalloporphyrin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Ferrochelatase in membrane preparations fromAzospirillum brasilense displayed an activity of 2.17 μmol protoheme formed · h−1 · mg protein−1 which is 10-fold greater than previous reports for other bacteria. This ferrochelatase showed an apparentK m of 20.9 μM for Fe2+, a pH optimum of 6.0–6.5, and stimulation by oleic or stearic acids. Co2+, Cu2+ and Zn2+ inhibited the incorporation of Fe2+ into protoporphyrin IX while Ni2 and Mg2+ had no effect on protoheme synthesis. Activity with Fe2+ and mesoporphyrin IX was less than with protoporphyrin IX but deuteroporphyrin IX produced the highest rate of protoheme synthesis. The membrane fraction containing ferrochelatase activity was found to insert Cu2+, Ni2+, Zn2+ and Co2+ enzymatically into protoporphyrin IX to produce metalloporphyrins. Cu2+ incorporation into protoporphyrin IX proceeded at a rate greater than with Fe2+ and theK m for Cu2+ was 21.9 μM.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01116198
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    Paper (German National Licenses)
    Fulltext
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