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Most immunologic tests currently in use depend upon the detection and quantitation of some result of the union of antigen and antibody. Such consequences of union include precipitation, agglutination, complement fixation and hemolysis. It is evident that the union of antigen and antibody precedes and is a necessary condition for the occurrence of these and other secondary phenomena. There have always been excellent reasons to believe that antigen could combine with antibody without the occurrence of such secondary reactions. A major difficulty in certain types of immunologic work in the past has been the necessity of determining the presence or the amount of antibody by measurement of the result of its union with the antigen rather than by the direct measurement of such a combination itself. A method which permits direct measurement of the union of antigen and antibody has obvious value for the study of systems where secondary reactions are either nonexistent or difficult to measure. The antibody which combines with insulin and which is the subject of this and the following paper is such an antibody. Its existence has long been suspected because of occasional local reactions to insulin and because of some of the biologic effects which the plasma of insulin treated patients has been known to possess. Until electrophoretic studies (1) demonstrated the combination of I131 insulin with gamma globulin of selected patients, there was no direct evidence of the existence of an antibody which combines with insulin in any human plasma. The recent work of Farr (2) demonstrating antibody with binding capacity for bovine serum albumin (BSA) stimulated the search for a similar method of demonstrating antibodies

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