Electrosyneresis (ES) was employed for the detection of enzyme-linked immunoglobulin.
ES is said to be unsatisfactory for detecting the cathodally migrating proteins such as immunoglobulins. When ES was carried out using the electrophoretic system in which serum application point was located in the middle of γ-globulin region, precipitin lines of IgA and of IgM could be formed on the anodic site of antigen (serum) application point and those of IgG on the cathodic and anodic site.
Non-precipitated enzyme was removed from the gel by pressing and enzyme staining was subsequently performed.
The method described here offers the following advantages: (1) The procedure is rapid; it takes 40min for the development of immunoprecipitin line and 30min for the removal of non-precipitated enzyme. (2) The detection of immunoglobulin is sensitive because it is based on ES. (3) Antiserum needed is minimal.
We compared the sensitivity of detecting LDH-linked immunoglobulins by ES, immunoelectrophoresis (IEP) and immunofixation (IF) using 28 sera with anomalous isoenzyme pattern. The frequency of identifing IgA was almost same in all methods, however, the number of IgG and light chains detected by ES was twice that of IF method and the sensitivity of IEP was intermediate that of ES and IF procedure.
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