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.
Subscribe to Journal
Get full journal access for 1 year
only $3.90 per issue
All prices are NET prices.
VAT will be added later in the checkout.
Tax calculation will be finalised during checkout.
Rent or Buy article
Get time limited or full article access on ReadCube.
All prices are NET prices.
Raben, M. S. J. clin. Endocr. 18, 901–904 (1958).
Goodman, H. G., Grumbach, M. M. & Kaplan, S. L. New Engl. J. Med. 278, 57–68 (1968).
Escamilla, R. F. in Hormonal Proteins and Peptides Vol. 3 (ed. Li, C. H.) 147–190 (Academic, London, 1975).
Raiti, S. (ed.) Proc. NIAMDD Symp. Publ. No. 74–612 (1973).
Lewis, U. J. et al. Recent Prog. Horm. Res. 36, 477–508 (1980).
Goeddel, D. V. et al. Nature 281, 544–548 (1979).
Burgess, R. R. & Jendrisak, J. J. Biochemistry 14, 4634–4638 (1975).
Laemmli, U. K. Nature 227, 680–685 (1970).
Li, C. H. in Hormonal Proteins and Peptides Vol. 3 (ed. Li, C. H.) 1–40 (Academic, London, 1975).
Clark, B. F. C. & Marcker, K. A. J. molec. Biol. 17, 394 (1966).
Cappechi, M. R. Proc. natn. Acad. Sci. U.S.A. 55, 1517–1524 (1966).
Adams, J. M. J. molec. Biol. 33, 571–589 (1968).
Li, C. H. in Hormonal Proteins and Peptides Vol. 4 (ed. Li, C. H.) 1–41 (Academic, London, 1977).
Stebbing, N. et al. Recombinant DNA tech. Bull. 3, 12–21 (1980).
Thorngren, K. G. & Hansson, L. I. Acta endocr., Copenh. 75, 653–668, 76, 35–52 (1974).
Hughes, P. C. R. & Tanner, J. M. J. Anat. 106, 349–370 (1970).
Holmstroem, B. & Fholenhag, K. J. clin. Endocr. Metab. 40, 856–862 (1975).
Lewis, U. J., Dunn, J. T., Bonewald, L. F., Seavey, B. K. & VanderLaan, W. P. J. biol. Chem. 253, 2679–2687 (1978).
Hirs, C. W. Meth. Enzym. 11, 59–62 (1967).
Gurd, F. R. N. Meth. Enzym. 11, 532–541 (1967).
Fullmer, C. S. & Wasserman, R. H. J. biol. Chem. 254, 7208–7212 (1979).
About this article
Cite this article
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
Changes in Manufacturing Processes of Biologic Therapies Can Alter the Immunogenicity Profile of the Product
Clinical Pharmacology & Therapeutics (2020)
Escherichia coli “TatExpress” strains export several g/L human growth hormone to the periplasm by the Tat pathway
Biotechnology and Bioengineering (2019)
High purity recombinant human growth hormone (rhGH) expression in Escherichia coli under phoA promoter
Microbial Cell Factories (2014)
Endocrine Practice (2012)