PaperThe binding of corroded metallic ions to salivary-type proteins
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<sup>1</sup>H NMR investigations of the molecular nature of cobalt(II) ions in human saliva
2012, Archives of Biochemistry and BiophysicsCitation Excerpt :Also of particular interest to this investigation is the observation that the salivary glycoprotein carbohydrate side-chain N-acetylsugar acetamido-CH3 (-NHCOCH3) group 1H NMR resonances were significantly and reproducibly broadened at added Co(II) concentrations >10−4 mol dm−3. This observation is consistent with the binding of this metal ion by such macromolecules, and interestingly, Mueller (1983) [72] found that both Cu(II) and Ni(II) were bound to a model glycoprotein at levels of 5.0 and 1.2 mol of metal ion per mol of protein, respectively, in a representative ‘inorganic’ salivary medium containing this macromolecular biomolecule, together with appropriate concentrations of mucin, amylase and lysozyme. Furthermore, this researcher postulated that these metal ions are complexed by N-acetylneuraminate carboxylate groups in the carbohydrate side-chains of the glycoprotein and mucin, and the imidazole ring of histidine residues present in amylase.
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2009, Food ChemistryCorrosion current between fresh and old amalgam
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1985, Science of the Total Environment, TheBinding of corroded ions to human saliva
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