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    Reaction of azide radicals with amino acids and proteins.

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    Authors
    Land, Edward J
    Prütz, W
    Affiliation
    Paterson Laboratories, Christie Hospital and Holt Radium Institute, Manchester
    Issue Date
    1979-07
    
    Metadata
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    Abstract
    The azide radical N3 reacts selectively with amino acids, in neutral solution preferentially with tryptophan (k (N3 + TrpH) = 4.1 X 10(9) dm3 mol(-1s-1) and in alkaline solution also with cysteine and tyrosine (k(N3 + CyS-) = 2.7 X 10(9) dm3 mol-1s-1) and k(N3 + TyrO-) equals 03.6 X 10(9) dm3 mol-1s-1). Oxidation of the enzyme yADH by N3 involves primary attacks, mainly at tryptophan residues, and subsequent slow secondary reactions. N3-induced inactivation of yADH is likely to occur upon oxidation of tryptophan residues in the substrate binding pocket (58-TrpH and 93-TrpH) since the substrate ethanol although unreactive with N3, protects yADH and since elADH, which does not contain tryptophan in the substrate pocket, is comparatively resistant against N3-attack. N3 exhibits low reactivity with nucleic acid derivatives and it is inert towards aliphatic compounds such as methanol and sodium dodecylsulphate.
    Citation
    Reaction of azide radicals with amino acids and proteins. 1979, 36 (1):75-83 Int J Radiat Biol Relat Stud Phys Chem Med
    Journal
    International journal of radiation biology and related studies in physics, chemistry, and medicine
    URI
    http://hdl.handle.net/10541/135876
    DOI
    10.1080/09553007914550831
    PubMed ID
    40916
    Type
    Article
    Language
    en
    ISSN
    0020-7616
    ae974a485f413a2113503eed53cd6c53
    10.1080/09553007914550831
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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