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Cryoimmunoglobulins are pathological antibodies characterized by a temperature-dependent reversible insolubility. Rheumatoid factors (RF) are immunoglobulins possessing anti-immunoglobulin activity and usually consist of an IgM antibody that recognizes IgG as antigen. These proteins are present in sera of patients affected by a large variety of different pathologies, such as HCV infection, neoplastic and autoimmune diseases. Aggregation and precipitation of cryoimmunoglobulins, leading to vasculiti, are physical phenomena behind such pathologies. A deep knowledge of the physico-chemical mechanisms regulating such phenomena plays a fundamental role in biological and clinical applications. In this work, a preliminary investigation of the aggregation kinetics and of the final macromolecular structure of the aggregates is presented. Through static light scattering techniques, the gyration radius Rg and the fractal dimension Dm of the growing clusters have been determined. However, while the initial aggregation mechanism could be described using the universal reaction-limited cluster–cluster aggregation (RLCCA) theory, at longest times from the beginning of the process, the RLCCA theory fails and a restructuring of clusters is observed together with an increase of the cluster fractal dimension Dm up to a value Dm∼3. The time tn, at which the restructuring takes place, and the final cluster size can be modulated by varying the quenching temperature. |
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