The disulphide bonds of insulin
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In order to deduce the unique structure of ox insulin it is necessary to know its molecular weight.In previous papers a value of 12 000 was assumedc since physical measurements suggested that this was the weight of the smallest unit that existed in solution, Recently, however, Harfenist & Craig (1952) have used a new chemical method and have found a value of approximately 6000.It is difficult to see how this result could be wrong and some recent physical measurements have shown that dissociation into units of molecular weight lower than 12 000 definitely occurs (Fredericq, 1953; Kupke & Linderstrom-Lang, 1954).It may thus safely be concluded that the molecular weight of insulin is 5734, on the basis of condensation of the amino acids present with normal elimination of water.This molecule is composed of two poly- peptide chains joined together by the disulphide bridges of three cystine residues.Treatment with performic acid splits the insulin to two fractions A and B, which are the oxidized forms of the glycyl and the phenylalanyl chain respectively (Sanger, Table 3. Jy8teic acid peptides obtained from crude 'tryptic' hydroly8ate of insuin (Expt.Ix)
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Frederick Sanger determined the amino acid sequences of the A and B chains of insulin; by 1955 he demonstrated the position of the two disulfide bonds linking the A and B chains and the intrachain disulfide bond within the A chain.
“In the early 1950s, Frederick Sanger determined the amino acid sequences of the A and B chains of insulin87–90. By 1955, he would demonstrate the position of the two disulfide bonds linking the A and B chains and the intrachain disulfide bond within the A chain, and in 1958, he was awarded the Nobel Prize in Chemistry91–93.”
From 100 years of insulin: celebrating the past, present and future of diabetes therapy (2021) · cites this paper as [92]
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Research works printed but not linked: 1
- Peters, J. P. & Van Slyke, D. D. (1932). Quantitative Clinical Chemi8try. Vol. 2, p. 385. London: Bailliere, Tindall and Cox.
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100 years of insulin: celebrating the past, present and future of diabetes therapy
Sims, E. K., Carr, A. L. J., Oram, R. A., DiMeglio, L. A., & Evans-Molina, C. (2021) · Nature Medicine · doi:10.1038/s41591-021-01418-2 · Cited by 270 · see citing works
Sanger, F. (1959) · Science · doi:10.1126/science.129.3359.1340 · Cited by 255 · see citing works
Self-citationProinsulin and C-peptide: A review
Kitabchi, A. E. (1977) · Metabolism · doi:10.1016/0026-0495(77)90099-3 · Cited by 140 · see citing works
- Authors
- Ryle, A. P., Sanger, F., Smith, L. F., & Kitai, R.
- Affiliations
- University of Cambridge (GB)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1955-08-01
- Volume
- 60
- Issue
- 4
- Pages
- 541-556
- ISSN
- 0306-3283 (ISSN-L)
- PMC
- PMC1216151
- OpenAlex
- W2414829511
- Cited by
- 927
- References
- 0
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 6 · 2023: 4 · 2022: 28 · 2021: 16 · 2020: 5 · 2019: 10 · 2018: 9 · 2017: 10 · 2016: 6 · 2015: 11 · 2014: 11 · 2013: 8 · 2012: 6
- FWCI
- 82.40
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Surgery › Pancreatic function and diabetes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- insulin, disulfide bonds, molecular weight, insulin structure, cystine residues, insulin A chain, insulin B chain, performic acid oxidation
- MeSH terms
- Disulfides, Insulin, Sulfides
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