FUSED ROCKET IMMUNOELECTROPHORETIC ANALYSIS OF HUMAN AND SHEEP THYROGLOBULINS PURIFIED BY GEL CHROMATOGRAPHY

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Abstract
Summary: The application of fused rocket immunoelectrophoretic methods for the analysis of human and sheep thyroid extracts is reported. Different experimental procedures, evaluating thyroglobulin preparations obtained by gel chromatographic separations with a variety of gel supports and elution conditions, were examined. Adsorption experiments demonstrated that many of the antigenic contaminants in chromatographed thyroglobulin were due to serum proteins. The precipitin profiles obtained with the fused rocket immunoelectrophoretic experiments indicate that considerable tailing of 19S‐thyroglobulin occurs when chromatographed on either Sephadex G‐200 or Bio‐Gel A‐1.5m using low ionic strength buffers. The retention of thyroglobulin on these supports would account, in part, for the observed presence of thyroid proteins with antigenic determinants identical to 19S‐thyroglobulin in chromatographed subfractions of notionally lower molecular weight. Because of the case of execution, the described methods provide a useful alternative to existing methods for the assessment of homogeneity of chromatographed thyroglobulin samples.