Abstract
SummaryThe human gamma globulin preparation studied in this investigation was dissolved in diluted phosphate buffer pH = 8.15 and divided into 3 subfractions by stepwise elution from anion-exchange cellulose. These showed different mean migration rate in starch gel electrophoresis. In conformity with the original preparation the subfractions were found to be active as reactant in the latex fixation test in dilutions containing at least 3 mcgr. of protein per ml.
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