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Multiplicity of Insulin Binding Antibodies in Human Sera

Presence of Antibody Activity in -, _2A-, and _2M-Globulins¹

From the Department of Biochemistry Research, Roswell Park Memorial Institute, New York State Department of Health, Buffalo 3, New York and Allergy Research Laboratory and Diabetic Clinic, Buffalo General Hospital and the Department of Medicine of the State University of New York at Buffalo, School of Medicine, Buffalo, New York

Abstract

1. Insulin-binding antibodies in human sera were studied with respect to their immunoelectrophoretic and chromatographic properties. The reagents used for developing precipitate arcs in immunoelectrophoresis were mixtures of a trace amount of I¹³¹ insulin and rabbit antiserum against particular components of human serum. Arcs formed by reaction of rabbit antibody and insulin-binding components of human serum fix I¹³¹ insulin and can be revealed by radioautography. The method is simple and extremely sensitive. In addition, the nature of insulinbinding components can be readily identified by comparing the radioautograph with the stained slide.

2. Fifteen out of 18 sera from diabetic patients under insulin treatment contained detectable amounts of insulin-binding components, presumably antibodies. (Three negative sera had been obtained from patients receiving less than 30 units insulin daily.) Sera from three insulin-allergic patients also contained insulin-binding antibodies. None of the sera from normal donors and diabetic patients who had never received insulin showed such components.

3. In the majority of the sera tested, the insulin-binding activity was found only in the -globulin. However, a serum from an insulin-allergic patient had the activity in the _2A- and _2M-globulins in addition to the -globulin. Another serum from an insulin-insensitive patient (requiring 90 units daily) also showed the detectable activity in the _2A-globulin.

4. Antibodies of the -globulin type were further separated into two distinctly different fractions by chromatography on diethylaminoethyl cellulose. These two fractions differed in their electrophoretic mobility (migrating in the ₁- and ₂-globulin regions respectively), but reacted in an identical manner against rabbit antiserum. The binding characteristics of these fractions to I¹³¹ labeled bovine zinc insulin were quite similar to each other.

Footnotes

¹ Supported in part by Grant No. H 2092, from the National Heart Institute and Grant No. E 1303 from the National Institute of Allergy and Infectious Diseases, United States Public Health Service.

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