The Biosynthesis of C14- and H3-Labeled Insulin

  • G. Eric Bauer
  • Arnold W. Lindall
  • Arnold Lazarow


In recent years, there has been much interest in the biosynthesis of insulin because of its role in diabetes. In addition, the exact amino acid sequence of the two peptide chains is known [1] and, therefore, the insulin molecule has become a model protein for research in synthetic mechanisms. Many techniques for the purification and characterization of insulin have been developed [2,3,4]. In the study of insulin biosynthesis, several investigators have incubated mammalian pancreas slices in the presence of radioactive amino acids in vitro, and then isolated the labeled insulin [3,5,6] This approach is limited because the beta cells of the islets of Langerhans (which manufacture and store insulin) comprise only a small fraction of the total pancreas. During the development of the pancreas in certain teleost fish, however, the islet tissue becomes separated from the exocrine pancreas and it appears in the adult as a macroscopic aggregate of endocrine tissue called the principal islet or Brockmann body. The principal islet contains cells which are functionally and anatomically analogous to the B-cells of mammalian islets; fish insulin is similar to mammalian insulin in structure and in biological activity [7,8]. Our studies on insulin biosynthesis using fish islets were begun in 1959; this report is a summary of these investigations.


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  1. 1.
    Sanger, F., and Smith, L. F., Endeavour 16: 48 (1957).Google Scholar
  2. 2.
    Romans, R. G., Scott, D. A., and Fisher, A. M., Ind. Eng. Chem. 32: 908 (1940).CrossRefGoogle Scholar
  3. 3.
    Light, A., and Simpson, M. V., Biochim. Biophys. Acta 20: 251 (1956).CrossRefGoogle Scholar
  4. 4.
    Harfenist, E. J., and Craig, L. C., J. Am. Chem. Soc. 74: 308 (1952).CrossRefGoogle Scholar
  5. 5.
    Pettinga, C. W., and Rice, C. N., Federation Proc. 11: 268 (1952).Google Scholar
  6. 6.
    Vaughan, M., and Anfinsen, C. B., J. Biol. Chem. 211: 367 (1954).PubMedGoogle Scholar
  7. 7.
    Macleod, J. J. R., J. Metab. Res. 2: 149 (1922).Google Scholar
  8. 8.
    Wilson, S., and Dixon, G., Nature 191: 876 (1961).CrossRefGoogle Scholar
  9. 9.
    Bauer, G. E., Doctral dissertation: University of Minnesota (1963).Google Scholar
  10. 10.
    Bauer, G. E., and Lazarow, A., Biol. Bull. 121: 425 (1961).CrossRefGoogle Scholar
  11. 11.
    Grodsky, G., and Tarver, H., Nature 177: 223 (1956).CrossRefGoogle Scholar
  12. 12.
    Lindall, A. W., Jr., Bauer, G. E., Dixit, P. K., and Lazarow, A., J. Cell Biol. 19: 317 (1963).CrossRefGoogle Scholar
  13. 13.
    Lazarow, A., Bauer, G. E., and Lindall, A W, Jr., in: The Structure and Metabolism of Pancreatic Islets ( S. E. Brolin, ed.), Pergamon Press, New York (1964).Google Scholar
  14. 14.
    Humbel, R. E., Biochim. Biophys. Acta 74: 96 (1963).CrossRefGoogle Scholar

Copyright information

© New England Nuclear Corporation 1965

Authors and Affiliations

  • G. Eric Bauer
    • 1
    • 2
  • Arnold W. Lindall
    • 1
    • 2
  • Arnold Lazarow
    • 1
    • 2
  1. 1.Department of AnatomyUniversity of MinnesotaMinneapolisUSA
  2. 2.Marine Biological LaboratoryWoods HoleUSA

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