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A number of anti-insulin factors present in the serum of insulin-resistant subjects has been reported. Lowell (1) presented evidence for both insulin-neutralizing and insulin-sensitizing antibodies. De Fillipis and lannaccone (2) and Colwell and Weiger (3) employing salting out methods and Sehon, Kaye, McGarry, and Rose (4) using starch electrophoresis have reported that insulin-neutralizing activity is localized in the y globulin fraction of the serum. Loveless and Cann ((5), utilizing the technique of electrophoresis convection, observed that insulin-blocking antibody is present in the y globulin.fraction while insulin-sensitizing antibody is recovered with the ,8 globulins. An anti-insulin factor, capable of inhibiting glycogen accumulation by the isolated rat diaphragm, was reported by Field and Stetten (6) to be present in the a and /3 globulin fraction of the serum of diabetic subjects, during episodes of severe insulin-resistant acidosis. In addition to the factors reported in cases of insulin resistance, an insulin-binding antibody has been demonstrated, by zone electrophoresis and ultracentrifugal fractionation studies employing insulin-I131, to be present consistently in the serum of insulin treated subjects (7, 8). A study of the distribution of insulin-binding antibody among serum fractions separated with cold ethanol revealed that antibody was restricted to fraction I + III (which is comprised chiefly of /8 and a globulins) in most subjects (9). In some, antibody was recovered in fraction II (primarily y globulins with a small amount of /l2 globulin) as well as in fraction I + III. In two subjects there were observed a small amount of insulin binding in fraction IV VI (mainly albumin with a small amount of ,8 and a globulins) as well as more marked binding in the other two fractions. In all cases, bound insulin migrated in the inter -y 8 region on electrophoresis, regardless of the fraction in which the antibody was recovered (9). Still another anti-insulin effect is manifested by some sera in inhibiting the degradation of insulin by rat liver homogenates. Williams (10) has recently reported that such inhibition is exhibited by normal plasma but that inhibition is much greater with diabetic than with normal sera. The different methods employed in the demonstration of anti-insulin factors and in the fractionation of serum for their localization have made it impossible to clearly differentiate among these factors. In the present study the plasma factor associated with apparent inhibition of liver insulinase has been identified with insulin-binding antibody. Inhibitory activity was not observed in normal plasma or in plasma of diabetic subjects who had never received exogenous insulin. The apparent inhibition of liver insulinase activity described in the present report is clearly to be distinguished from that due to direct interference with the liver insulinase system. Inhibition in the present sense applies solely to the protection of insulin from the degrading action of liver insulinase as a consequence of the binding of insulin by insulinbinding antibody.

APPARENT INHIBITION OF LIVER INSULINASE ACTIVITY BY SERUM AND SERUM FRACTIONS CONTAINING INSULIN-BINDING ANTIBODY