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  • Title: Reaction of osmium reagents with amino acids and proteins. Reactivity of amino acid residues and peptide bond cleavage.
    Author: Deetz JS, Behrman EJ.
    Journal: Int J Pept Protein Res; 1981 Apr; 17(4):495-500. PubMed ID: 7309353.
    Abstract:
    We report a study of the relative reactivity of the common amino acids and of their residues in lysozyme with osmium tetroxide, the osmium tetroxide-pyridine reagent, and with the oxo-osmium(VI)-pyridine reagent. With free amino acids, the osmium(VIII) reagents are most reactive with Met, Cys, His, Thr, Ser, Trp, Lys, and Pro; the osmium(VI) reagent only reacts significantly with His, Met, Cys, Thr, and Ser. In lysozyme, only Cys, Met, and Trp react extensively with the osmium(VIII) reagents; with the osmium(VI) reagent, Cys and Met are most reactive. We also note evidence both for cross-linking of proteins and for peptide bond cleavage, which appears to have considerable specificity for tryptophanyl residues.
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