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.
Keywords
ProinsulinTrypsinSedimentation equilibriumBiochemistryAmino acidPeptideChemistryPeptide sequenceInsulinCleavage (geology)StereochemistryBiologyUltracentrifugeEnzymeEndocrinology
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Publication Info
- Year
- 1968
- Type
- article
- Volume
- 161
- Issue
- 3837
- Pages
- 165-167
- Citations
- 319
- Access
- Closed
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Cite This
Ronald E. Chance,
Robert M. Ellis,
William Bromer
(1968).
Porcine Proinsulin: Characterization and Amino Acid Sequence.
Science
, 161
(3837)
, 165-167.
https://doi.org/10.1126/science.161.3837.165
Identifiers
- DOI
- 10.1126/science.161.3837.165