Abstract
An efficient method of separating proteins by electrophoresis with agarose gels containing sodium dodecyl sulfate is described. The separated proteins were then used to make antibodies. The separation of proteins in the molecular weight range 25K to 94K on 4 to 5% agarose gels showed good resolution which was comparable to that obtained by electrophoresis with polyacrylamide gels containing sodium dodecyl sulfate. The subunits of human chorionic gonadotropin were separated by the preparative agarose gel electrophoresis and the gel bands containing the subunits were used directly to raise antibodies against these proteins. The degree of solubilization of the proteins from the gel slices was found to be complete.
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