One of the uses of serum protein electrophoresis is in detecting a monoclonal gammopathy, the presence of which can indicate a range of related conditions associated with immunoglobulin production.
Electrophoresis allows separation of macromolecules in solution by application of an electrical field. The serum protein electrophoresis (SPE) test represents the most widespread application of the technique in routine clinical laboratories. Serum is applied to a buffered agarose gel and an electric current is applied to the gel. Under the conditions of the test, the many thousands of proteins present in serum are separated according to size and charge to one of five fractions, which are, in order of electrophoretic mobility towards the positive electrode (anode): albumin, α1-globulin, α2-globulin, β-globulin and γ-globulin.
Electrophoresis systems exhibiting the best resolution can distinguish two β-globulin fractions (β1- and β2-globulin). Staining of the gel with a protein-specific stain allows visualisation of the five (or six) fractions. As density of staining is proportional to protein concentration, densitometric scanning of the stained gel allows a graphical display of the five fractions and quantitation of the relative concentration of each fraction. If the total serum protein concentration is available, the absolute concentration of each fraction can be determined. Increase or decrease in any of the five fractions has clinical/diagnostic significance, but the focus here is increase in the γ-globulin fraction.
Gammopathy
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