Abstract
Patterns obtained by electrophoresis of human serum on starch gel have shown the presence of 14 to 30 protein components. Of these, only one starch gel fraction has been attributed to serum albumin. As the urea concentration approached 6 M only 4–5 protein components were visible. These serum fractions obtained from electro-phoresis on 6 M urea-starch gels appeared similar in mobility, intensity and configuration to those obtained by electrophoresis of purified human serum albumin. Two-directional immunodiffusion and immunoelectrophoretic analyses show that these fractions represent protein components immunologically identical to albumin. Serum globulin components appeared to be present in only trace amounts. These experiments suggest that when human serum is run electrophoretically on starch gel containing 6 M urea, a series of homologous protein appear on the gel which may differ in molecular size or shape, but all of which share antigenicity with serum albumin.
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