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Ch2 recombinant

Simple explanation of how human insulin is made using an e. coli process to clone it.

This long abbreviation refers to any insulin made using biotechnology. These are human insulins at present.

r-DNA is the type of process used, GE or GM refer to the resulting type of insulins. Since only human insulin has a large enough market for this expensive effort, all r-DNA insulins are human insulins or analogs (altered insulins). r-DNA processes could in theory be used to make animal insulins as well.

Human insulins you can buy are genetically engineered (GE) insulins or Analog insulins, which are human structure insulins which have various alterations of their amino acids.

Biotech was first used to change pork insulin to human insulin by substituting one amino acid (Alanine at B30 to Threonine). [1][2][3][4] The result was a Genetically Modified (GM) insulin.

Novo Nordisk produced its human insulins this way from 1981 to 1988. [5] Genetic modification fell out of favor because genetic engineering became less costly. Beta Laboratorios produces their Betalin line of human insulins this way; [6] they are one of the few insulin manufacturers still producing a human Lente insulin.

Biosynthesis, or Genetic Engineering, is currently cheaper than GM. The gene for human insulin (r-DNA) is spliced, or inserted into an organism [7] such as e. Coli (bacteria)[8] or yeast[9] made with a special type of genetically engineered wheat.

Various biotechnical processes then induce the bacteria or yeast to produce human insulin, which is harvested, processed and purified.

Novo Nordisk uses the wheat/yeast process for its insulins; [10] Eli Lilly [11] and Aventis [4] each use e. Coli bacteria and their own patented process to produce their insulins.

Lilly was the first pharmaceutical firm to produce any biosynthetic human insulin. Novo Nordisk was the first to produce human insulin outside of the human body; [5] they initially used the semi-synthetic process described above.

You see here that r-DNA insulin is produced to be a perfect amino acid match to that a human being's body produces naturally. The insulin is one amino acid away from a perfect match to both dog and pig insulin--humans have Threonine at the #30 position on the B insulin chain, while dogs and pigs have Alanine there. For comparing bovine insulin, humans and cows have only the #18 position on the A insulin chain in common, both having Asparagine there. So human and bovine insulins differ by 3 amino acids.

R-DNA/GE/GM Insulins[]


  1. Insulin Therapy-Overview.
  2. Raptis S, Dimitriadis G. (1985). Human Insulin. Clinical Physiology & Biochemistry.
  3. Rose, Keith, et. al. (1991). Technical Description of Human Insulin by Semi-Synthetic Process. Oxford Journals.
  4. 4.0 4.1 Scientific Discussion-Insuman-Page 1. EMEA. Cite error: Invalid <ref> tag; name "EMEA" defined multiple times with different content
  5. 5.0 5.1 Human Insulin. Novo Nordisk UK. Cite error: Invalid <ref> tag; name "Novo" defined multiple times with different content
  6. Beta Laboratorios. Beta Laboratorios.
  7. Transfer & Cloning of the Insulin Gene. National Health Museum.
  8. Insulin. American Chemical Society.
  9. Raskin P, Clements RS Jr. (1991). The use of human insulin derived from baker's yeast by recombinant DNA technology.. Clinical Therapeutics.
  10. Patient Information Leaflet-Novolog-Page 1. Novo Nordisk.
  11. Humulin R Patient Information Leaflet. Eli Lilly.
  12. Guide to Insulin Preparations. Pharmacy Times.

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