Oxidation of Insulin by Performic Acid

@article{Sanger1947OxidationOI,
  title={Oxidation of Insulin by Performic Acid},
  author={Frederick Sanger},
  journal={Nature},
  year={1947},
  volume={160},
  pages={295-296}
}
  • F. Sanger
  • Published 30 August 1947
  • Chemistry, Biology
  • Nature
FROM the determination of the terminal residues of insulin, it was suggested that the submolecule of molecular weight 12,000 is made up of four peptide chains bound together by —S—S— linkages1. Thus if one could break the —S—S— linkages without affecting any other part of the molecule, it should be possible to split the insulin into its separate poly-peptide chains, two of which have terminal glycyl residues and the other two phenylalanyl residues. Toennies and Homiller2 showed that the only… 
Some Peptides from Insulin
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It has been possible to prepare two fractions from the oxidized insulin: fraction A contains only glycine terminal residues and no arginine, histidine, lysine, phenylalanine or threonine; fraction B contains 97 per cent phenolalanine terminal residue and all the amino-acids that are present in insulin.
The reaction of iodate with cystine and with insulin.
The Core of the Insulin Molecule
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The facts suggest that the basic unit of insulin is a molecule of molecular Weight 12,000, which is probably better known than that of any other protein.
The Chemical Composition and Structure of Wool
The first two amino acids to be isolated from protein hydrolysates were glycine and leucine, both by Braconnot and both in 1820.(1) Of these two, leucine was isolated from wool, which can thus lay
Identification of unusually disulphide-bonded insulin forms using mass spectrometry and thermolysin cleavage
TLDR
Using the endoplasmic stress inducer, thapsigargin, this approach lays foundations to identify the scope and cause of aberrant insulin disulphide formation in health and disease.
Reaction of cysteine thiol groups with 1,3-propane sultone: S-3-sulphopropyl as a modifying group for protein chemistry.
TLDR
S-3-Sulphopropylcysteine is stable to the conditions to total acid hydrolysis and behaves distinctively in electrophoresis and ion-exchange chromatography.
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The free amino groups of insulin.
  • F. Sanger
  • Biology, Medicine
    The Biochemical journal
  • 1945