Porcine Proinsulin: Characterization and Amino Acid Sequence
Abstract
Proinsulin in nearly homogeneous form has been isolated from a preparation of porcine insulin. A molecular weight close to 9100 was calculated from the amino acid composition and from sedimentation-equilibrium studies. Through the action of trypsin this single-chain protein is transformed to desalanine insulin by cleavage of a polypeptide chain connecting the carboxy-terminus of the B chain to the amino-terminus of the A chain of insulin. The amino acid sequence of this connecting peptide was found to be Arg-Arg-Glu-Ala-Gln-Asn-Pro-Gln-Ala-Gly-Ala-Val-Glu-Leu-Gly-Gly-Gly-Leu-Gly-Gly-Leu-Gln-Ala-Leu-Ala-Leu-Glu-Gly-Pro-Pro-Gln-Lys-Arg.
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In 1968, Ronald Chance published the porcine sequence of the proinsulin molecule.
“In 1968, Ronald Chance at Lilly Research Laboratories in Indianapolis published the porcine sequence of the proinsulin molecule96.”
From 100 years of insulin: celebrating the past, present and future of diabetes therapy (2021) · cites this paper as [96]
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- Authors
- Chance, R. E., Ellis, R. M., & Bromer, W. W.
- Affiliations
- Eli Lilly (United States) (US)
- Venue
- Science
- Published
- 1968-07-12
- Volume
- 161
- Issue
- 3837
- Pages
- 165-167
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2093477186
- Cited by
- 320
- References
- 0
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 2 · 2023: 4 · 2022: 2 · 2021: 4 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 1 · 2015: 3 · 2014: 1 · 2013: 2 · 2012: 5
- FWCI
- 88.70
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- proinsulin, porcine insulin, amino acid sequence, C-peptide, trypsin cleavage, molecular weight, sedimentation equilibrium, polypeptide chains
- MeSH terms
- Amino Acid Sequence, Animals, Biological Assay, Cellulose, Chromatography, Ion Exchange, Chymotrypsin, Electrophoresis, Disc, Hypoglycemia, Insulin, Molecular Weight, Peptides, Proteins, Seizures, Swine, Trypsin
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