History of Insulin


Type 1 diabetes mellitus is an endocrine disorder in which the pancreas fails to produce the peptide hormone insulin, which is necessary for the regulation of glucose metabolism. Before the advent of insulin treatment, the condition was invariably fatal. At the beginning of the twentieth century, aware of the accumulating evidence that the hyperglycaemia of diabetes mellitus could be controlled by an extract of the pancreas, Banting and Best produced the first clinically useful insulin preparation at the University of Toronto.

Insulin research led to a number of important breakthroughs in biochemistry: insulin was the first protein to be sequenced, it was the first peptide hormone shown to be formed by a posttranslational transformation of an inactive precursor and it was also the first genetically engineered protein to be approved for clinical use.

Key Concepts

  • Control of blood glucose levels is vitally important for health, and these are regulated by the hormone insulin.
  • Insulin is a peptide hormone produced by the pancreas.
  • Insufficient insulin results in the endocrine disease, diabetes mellitus.
  • Hyperglycaemia and glycosuria (glucose in urine) are important signs of diabetes mellitus.
  • Insulin and C‐peptide are produced by cleavage of proinsulin, a precursor protein.
  • Pharmaceutical insulin preparations do not currently contain C‐peptide.

Keywords: insulin; diabetes mellitus; hyperglycaemia; pancreas; peptide hormone; C‐peptide


Abel JJ (1926) Crystalline insulin. Proceedings of the National Academy of Sciences of United States of America 12: 132–136.

Banting FG, Best CH, Collip JB, Campbell WR and Fletcher AA (1922) Pancreatic extracts in the treatment of diabetes mellitus. Preliminary report. Canadian Medical Association Journal 12: 141–146.

Hagedorn HC, Jensen BN, Krarup NB and Wodstrup I (1936) Protamine insulinate. Journal of the American Medical Association 106: 177–180.

Keefer LM and Meyts PM‐AD (1981) Human insulin prepared by recombinant DNA techniques and native human insulin interact identically with insulin receptors. Proceedings of the National Academy of Sciences of United States of America 78 (3): 1391–1395.

Macleod J (1922) Insulin and diabetes. British Medical Journal 2: 833–835.

Pratt JH (1954) A reappraisal of researches leading to the discovery of insulin. Journal of the History of Medicine and Allied Sciences 9: 281–289.

Sanger F (1945) The free amino groups of insulin. Biochemical Journal 39: 507–515.

Sanger F (1949) The terminal peptides of insulin. Biochemical Journal 45: 563–574.

Sanger F and Tuppy H (1951) The amino‐acid sequence in the phenylalanyl chain of insulin. 2. The investigation of peptides from enzymic hydrolysates. Biochemical Journal 49: 481–490.

Sanger F and Thompson EO (1952) The amino‐acid sequence in the glycyl chain of insulin. Biochemical Journal 52 (1): i.2–xiii.

Scott DA and Fisher AM (1935) Crystalline insulin. Biochemical Journal 29: 1048–1054.

Steiner DF, Cunningham D, Spigelman L and Aten B (1967) Insulin biosynthesis: evidence for a precursor. Science 157 (3789): 697–700.

Wahren J, Ekberg K, Johansson J, et al. (2000) Role of C‐peptide in human physiology. American Journal of Physiology. Endocrinology and Metabolism 278: 759–768.

Further Reading

Bliss M (1982) The Discovery of Insulin. Chicago: University of Chicago Press.

Rosenfeld L (2002) Insulin: discovery and controversy. Clinical Chemistry 48 (12): 2270–2288.

Stretton AOW (2002) The first sequence: Fred Sanger and insulin. Genetics 162: 527–532.

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Dagen, Morag M(Jan 2016) History of Insulin. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1002/9780470015902.a0003623.pub2]