Horm Metab Res 1986; 18(7): 470-472
DOI: 10.1055/s-2007-1012348

© Georg Thieme Verlag, Stuttgart · New York

Can Insulin Antibodies of Diabetic Patients Distinguish Human Insulin from Porcine Insulin?

O. Ishibashi, M. Kobayashi, H. Maegawa, N. Watanabe, Y. Takata, Y. Okuno1 , Y. Shigeta
  • Third Department of Medicine, Shiga University of Medical Science, Ohtsu, Japan
  • 1Second Department of Internal Medicine, Osaka City University Medical School, Osaka, Japan
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Publication History



Publication Date:
14 March 2008 (online)


We examined antisera from patients treated with bovineporcine mixture (hereafter referred to as bovine/porcine), porcine or human insulin, and compared their binding affinities to human insulin with those to porcine insulin. Patients treated with bovine/porcine insulin developed antisera with a higher affinity to porcine insulin compared with that to human insulin in five of nineteen cases. Furthermore, three of these five antisera had a comparable affinity to bovine and porcine insulin and appeared to recognize the amino acid residue at B-30. Treatment with porcine or human insulin, on the other hand, did not result in any significant difference in the affinity to porcine and human insulin in twenty-three patients. These results indicate the significant role of B-30 amino acid residue as an antigenic determinant, and suggest that the amino acid sequence of the A chain of bovine insulin may contribute to the development of antibody recognizing B-30 amino acid residue.