Guinea pigs were immunized with regular insulin in Freund's adjuvant weekly (N = 6) or with NPH insulin daily (N = 10). The concentrations, the affinities, and the sizes of the insulin-immunoglobin G (IgG) antibody complexes were determined by ultracentrifugation. During the immune response to insulin, 7-S complexes were observed after 3 wk, and 10-S complexes were observed after 4 wk (2P < .05 in each group). “7-S” antibodies were transferred into immunized guinea pigs before the formation of measurable antibody concentrations. The development of 10-S structures was enhanced in outbred Pirbright white guinea pigs (2P < .05, N = 6) and in inbred strain II l.b.m. guinea pigs (2P < .05, N = 7). Insulin may act as a monovalent antigen (7 S) after 3 wk and become bivalent after 4 wk (10 S). The change in valency is enhanced by antibody transfer. It reflects the formation of antibodies recognizing new epitopes on insulin.
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Original Contributions| December 01 1986
Maturation of Immune Response to Insulin: Recruitment of New Epitopes by Antibodies
K -G Petersen;
Address reprint requests to Karl-Georg Petersen, Hugstetter Strasse 55, D-7800 Freiburg, FRG.
K -G Petersen, G Schuler, W Hösl, M-J Storch, L Kerp; Maturation of Immune Response to Insulin: Recruitment of New Epitopes by Antibodies. Diabetes 1 December 1986; 35 (12): 1321–1325. https://doi.org/10.2337/diab.35.12.1321
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