Abstract
A relatively rapid technique for the isolation of human IgD myeloma proteins from whole sera is described. It is based on the use of the newly available Ultragel AcA34 gel filtration medium which yields a very substantially purified IgD fraction from whole serum. The absence of IgG from this fraction allows further purification on DEAE celulose under conditions where the IgD protein is not absorbed but other protein contaminants are retained. The overall yield of IgD protein is estimated at > 90% and the technique is particularly applicable to the isolation of IgD from small serum volumes.
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