When analyzing serum samples in clinical laboratory, we encounter analytical interference. As we mixed serum with sour demineralized water we discovered an interesting phenomenon of precipitation of serum proteins and we soon connected it with monoclonal gammopathy. Appearance of monoclonal immunoglobulin in serum is reflected as a consequence of a group of disease conditions. Because of the unusual features of precipitated proteins and their connection to patology, we named them paraproteins with unusual feature of precipitation. Because proteins do not precipitate in this conditions, we were interested in features and composition of this paraprotein and the reason for its precipitation.
Research method
In our research we isolated a paraprotein with unusual feature of precipitation and separated it on protein fractions with capillary electrophoresis. With two-dimensional gel electrophoresis we made paraprotein proteomic profile and determined molecular weight of paraprotein’s fragments. With mentioned methods we tried to identify paraprotein and learn as much as possible about its features. Theoretical part of the research is statistical analysis of biomarkers for serum samples with unusual feature of precipitation and samples with monoclonal immunoglobulin without precipitation of paraprotein.
Result
In our research we found the differences between samples of serum with monoclonal immunoglobulin without precipitation and serums with precipitations of paraprotein. Results of capilaryis electroforesis showed that a larger proportion of paraprotein has a shape of monoclonal immunoglobulin. Immuno complexes on paraprotein proteingrams were not visible. Proteomic profiles of paraprotein are suggesting the presence of heavy chains and light chains of immunoglobulin. Mass spectrum of paraprotein samples showed a mixture of several very large protein molecules, but we couldn't determine molecular weight to larger molecules, due to the limitations of our method.
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