Influence of heavy metal ions on antibodies and immune complexes investigated by dynamic light scattering and enzyme-linked immunosorbent assay

Bauer, Rogert; Müller, Achim; Richter, M.; Schneider, Klaus; Frey, Jürgen; Engelhardt, Waltraud

doi:10.1016/s0304-4165(96)00078-5

Cited by 21 publications

(13 citation statements)

References 29 publications

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“…Published data indicate that a 10-fold molar excess of copper does not reduce the antigen-binding activity of antibodies [9]. The hypothesis on the probability of these changes is fully justified for our study.…”

Section: Resultssupporting

confidence: 49%

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Preparation of specimens of human serum γ-globulin modified by copper and zinc and its immunochemical characteristics

et al. 2006

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Specimens of human serum gamma-globulin modified by molar excess of copper and zinc cations were obtained by molecular ultrafiltration. Conformation characteristics of the protein were determined by UV spectrophotometry. Immunochemical study included radial immunodiffusion test and direct and sandwich enzyme-linked immunosorbent assay. After binding of copper and zinc, the gamma-globulin molecule underwent conformation changes modifying presentation of antigenic determinants on the globule surface and their availability for recognition by specific antibodies. The effects of copper were much more pronounced than those of zinc cations.

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Section: Resultssupporting

confidence: 49%

“…On the other hand, copper cations modifying proteins promote the formation of intra-and intermolecular bityrosine cross-links [5], cause aggregate formation [6,7,9], stabilize the appearing supra- molecular complexes under certain conditions [1], and, as components of ceruloplasmin, provide antioxidant defense [4].…”

Section: Resultsmentioning

confidence: 99%

Preparation of specimens of human serum γ-globulin modified by copper and zinc and its immunochemical characteristics

et al. 2006

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“…Even 10-fold excess of copper ions (not physiological number of cations per protein molecule) does not reduce antigen-binding activity of antibodies [8].…”

Section: Resultsmentioning

confidence: 96%

“…The formation of large insoluble aggregations of rat monoclonal IgG1 occurs in the presence of at least 4 Cu 2+ per protein molecule [8]. Even 10-fold excess of copper ions (not physiological number of cations per protein molecule) does not reduce antigen-binding activity of antibodies [8].…”

Section: Resultsmentioning

confidence: 98%

Formation of Supramolecular Aggregations of γ-Globulin as a Metal-Dependent Process

et al. 2005

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The presence of copper cations in the solution of human serum gamma-globulin induced the formation of supramolecular forms of the protein. The intensity of this reaction increased with increasing copper concentration. The mechanisms of g-globulin aggregate formation under normal conditions and the possible role of bivalent metal cations in the regulation of protein effector functions are discussed.

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“…Since the absolute majority of cations in circulation are bound to proteins, glycoproteins, and other plasma components [6,7,9,13], there are good grounds to expect that copper toxicity towards body cells does not manifest under physiological conditions [1], no metal-dependent protein aggregation takes place [2,5], and spontaneous aggregation is inhibited [7]. Cations can incorporate into the macromolecule structure [2,3,6,12,13], modify their conformation [2,3,6,9]; they also can penetrate into cells and bind to specific chaperones thus regulating the function of metal-dependent proteins [1].…”

mentioning

confidence: 99%

Antigenic specificity of human serum γ-globulin samples obtained under conditions of equimolar binding of copper and zinc cations

et al. 2007

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Samples of human serum gamma-globulin modified by equimolar binding of copper and zinc cations were obtained using the method of molecular ultrafiltration. Conformation characteristics of the protein were studied by UV spectrophotometry. Immunochemical study included radial immunodiffusion test, direct and sandwich enzyme immunoassays. Conformation changes in gamma-globulin caused by incorporation of solitary metal cations into the protein molecule modified presentation of antigenic determinants on the globule surface and their availability for recognition by specific antibodies. New antigenic determinants and new antigenic specificity of gamma-globulin are not formed under these conditions.

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Influence of heavy metal ions on antibodies and immune complexes investigated by dynamic light scattering and enzyme-linked immunosorbent assay

Cited by 21 publications

References 29 publications

Preparation of specimens of human serum γ-globulin modified by copper and zinc and its immunochemical characteristics

Preparation of specimens of human serum γ-globulin modified by copper and zinc and its immunochemical characteristics

Formation of Supramolecular Aggregations of γ-Globulin as a Metal-Dependent Process

Antigenic specificity of human serum γ-globulin samples obtained under conditions of equimolar binding of copper and zinc cations

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