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Comparative analytical studies on recombinant and native human somatotropin.

M Schleyer1, C Mayer

  • 1Proteinlabor der Abteilung Innere Medizin I, Universität Ulm.

Biological Chemistry Hoppe-Seyler
|October 1, 1990
PubMed
Summary

Recombinant somatotropin exhibits heterogeneity similar to native pituitary somatotropin, with variations in amino acid composition and the presence of dimers. This suggests complex post-translational modifications or cloning artifacts in the produced somatotropin.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biotechnology

Background:

  • Somatotropin (growth hormone) is crucial for growth and metabolism.
  • Native pituitary somatotropin is known to be heterogeneous.
  • Recombinant DNA technology is used to produce therapeutic proteins like somatotropin.

Purpose of the Study:

  • To compare the heterogeneity of somatotropin produced by recombinant DNA technology with native pituitary somatotropin.
  • To investigate the sources of heterogeneity in recombinant somatotropin, including deamination and dimerization.
  • To analyze the amino acid composition of cloned somatotropins and compare it to native and recognized human somatotropin.

Main Methods:

  • Polyacrylamide gel electrophoresis (PAGE) to assess protein heterogeneity.

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  • Isoelectric focusing (IEF) to analyze charge heterogeneity.
  • Quantitative amino acid analysis to determine protein composition.

    • Main Results:

    • Recombinant somatotropin displayed heterogeneity comparable to native pituitary somatotropin.
    • Heterogeneity was not solely due to deamination of a single molecular species.
    • Cloned products contained the main 22 kDa protein and traces of interchain disulphide dimers.
    • Quantitative amino acid analyses of cloned somatotropins differed from each other and from native hormone analysis.
    • Discrepancies were observed between the amino acid compositions of studied hormones and the recognized analysis for human somatotropin.

    Conclusions:

    • The heterogeneity observed in recombinant somatotropin mirrors that of native pituitary somatotropin.
    • The source of heterogeneity in recombinant somatotropin is complex, involving factors beyond simple deamination.
    • Amino acid composition analysis reveals significant differences, suggesting potential issues in recombinant production or characterization.