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Purified human growth hormone from E. coli is biologically active

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Abstract

Human growth hormone (HGH), somatotropin, is a protein consisting of 191 amino acids with a molecular weight of ∼22,000. It is essential for linear growth and its application in the treatment of hypopituitary dwarfism is well established1–3. Growth hormone may also be effective in the treatment of other disorders including bone fractures, burns and bleeding ulcers4. Because growth hormone is species specific, human cadavers have previously been the only source of HGH. Moreover, the standard purification of pituitary-derived HGH does not provide a homogeneous product, but rather a mixture of native HGH and modified forms and fragments of HGH, each of which may have different physiological roles5. The expression of HGH in Escherichia coli using recombinant DNA technology6 provides an inexhaustible source of a single eukaryotic protein. The bacterially synthesized HGH, produced from E. coli, is methionyl-HGH (Met-somatotropin), the extra methionine arising from the AUG start codon inserted at the beginning of the gene. This cloned product has now been purified to homogeneity and its biological properties examined. For pituitary and bacterially synthesized HGH, specific activities as determined by radioimmunoassay are comparable.

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References

  1. Raben, M. S. J. clin. Endocr. 18, 901–904 (1958).

    Article  CAS  Google Scholar 

  2. Goodman, H. G., Grumbach, M. M. & Kaplan, S. L. New Engl. J. Med. 278, 57–68 (1968).

    Article  CAS  Google Scholar 

  3. Escamilla, R. F. in Hormonal Proteins and Peptides Vol. 3 (ed. Li, C. H.) 147–190 (Academic, London, 1975).

    Google Scholar 

  4. Raiti, S. (ed.) Proc. NIAMDD Symp. Publ. No. 74–612 (1973).

  5. Lewis, U. J. et al. Recent Prog. Horm. Res. 36, 477–508 (1980).

    CAS  PubMed  Google Scholar 

  6. Goeddel, D. V. et al. Nature 281, 544–548 (1979).

    Article  ADS  CAS  Google Scholar 

  7. Burgess, R. R. & Jendrisak, J. J. Biochemistry 14, 4634–4638 (1975).

    Article  CAS  Google Scholar 

  8. Laemmli, U. K. Nature 227, 680–685 (1970).

    Article  ADS  CAS  Google Scholar 

  9. Li, C. H. in Hormonal Proteins and Peptides Vol. 3 (ed. Li, C. H.) 1–40 (Academic, London, 1975).

    Google Scholar 

  10. Clark, B. F. C. & Marcker, K. A. J. molec. Biol. 17, 394 (1966).

    Article  CAS  Google Scholar 

  11. Cappechi, M. R. Proc. natn. Acad. Sci. U.S.A. 55, 1517–1524 (1966).

    Article  ADS  Google Scholar 

  12. Adams, J. M. J. molec. Biol. 33, 571–589 (1968).

    Article  CAS  Google Scholar 

  13. Li, C. H. in Hormonal Proteins and Peptides Vol. 4 (ed. Li, C. H.) 1–41 (Academic, London, 1977).

    Google Scholar 

  14. Stebbing, N. et al. Recombinant DNA tech. Bull. 3, 12–21 (1980).

    CAS  Google Scholar 

  15. Thorngren, K. G. & Hansson, L. I. Acta endocr., Copenh. 75, 653–668, 76, 35–52 (1974).

    Article  CAS  Google Scholar 

  16. Hughes, P. C. R. & Tanner, J. M. J. Anat. 106, 349–370 (1970).

    CAS  PubMed  PubMed Central  Google Scholar 

  17. Holmstroem, B. & Fholenhag, K. J. clin. Endocr. Metab. 40, 856–862 (1975).

    Article  Google Scholar 

  18. Lewis, U. J., Dunn, J. T., Bonewald, L. F., Seavey, B. K. & VanderLaan, W. P. J. biol. Chem. 253, 2679–2687 (1978).

    CAS  PubMed  Google Scholar 

  19. Hirs, C. W. Meth. Enzym. 11, 59–62 (1967).

    Article  CAS  Google Scholar 

  20. Gurd, F. R. N. Meth. Enzym. 11, 532–541 (1967).

    Article  CAS  Google Scholar 

  21. Fullmer, C. S. & Wasserman, R. H. J. biol. Chem. 254, 7208–7212 (1979).

    CAS  PubMed  Google Scholar 

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Author notes

  1. Douglas Fodge and George Prender: SRI International, 333 Ravenswood Drive, Menlo Park, California 94025, USA

Authors and Affiliations

  1. Genentech Inc., 460 Point San Bruno Boulevard, South San Francisco, California, 94080, USA

    Kenneth C. Olson, James Fenno, Norman Lin, Richard N. Harkins, C. Snider, W. H. Kohr, Michael J. Ross, Douglas Fodge, George Prender & Nowell Stebbing

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  1. Kenneth C. Olson
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  2. James Fenno
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  3. Norman Lin
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  4. Richard N. Harkins
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  5. C. Snider
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  6. W. H. Kohr
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  7. Michael J. Ross
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  8. Douglas Fodge
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  9. George Prender
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  10. Nowell Stebbing
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Olson, K., Fenno, J., Lin, N. et al. Purified human growth hormone from E. coli is biologically active. Nature 293, 408–411 (1981). https://doi.org/10.1038/293408a0

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