Abstract
BY oxidation with performic acid, the insulin molecule can be split into its separate polypeptide chains1. It has now 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 phenylalanine terminal residues and all the amino-acids that are present in insulin. The yield of fraction A is more than 25 per cent of the original insulin, indicating that it represents more than one of the peptide chains of the insulin. The yield of fraction B is rather less.
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References
Sanger, F., Nature, 160, 295 (1947).
Woolley, D. W., Federation Proc., 7, 200 (1948).
Porter, R. R., and Sanger, F., Biochem. J., 42, 287 (1948).
Polson, A., Mosley, V. M., and Wyckoff, R. W. G., Science, 105, 603 (1947).
Consden, R., Gordon, A. H., and Martin, A. J. P., Biochem. J., 41, 590 (1947).
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SANGER, F. Some Peptides from Insulin. Nature 162, 491–492 (1948). https://doi.org/10.1038/162491a0
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DOI: https://doi.org/10.1038/162491a0
