Recombinant DNA-derived methionyl human growth hormone is similar in membrane binding properties to human pituitary growth hormone

Ron G. Rosenfeld, Bharat B. Aggarwal, Raymond L. Hintz, Laura A. Dollar

Research output: Contribution to journalArticle

17 Scopus citations

Abstract

N-terminal methionyl human growth hormone (met-hGH), expressed in Escherechia coli by recombinant DNA techniques, was compared to native human pituitary growth hormone in receptor-binding activity. Met-hGH was indistinguishable from pituitary hGH in binding to specific hGH receptors on cultured IM-9 lymphocytes and to "lactogenic" receptors on pregnant rat liver membranes. Additionally, met-hGH and pituitary hGH were equivalent in ability to induce hGH receptor loss in IM-9 cells, with an 80% decrease in membrane binding sites following 20 hour preincubation with 10 ng/ml of either met-hGH or pituitary hGH. We conclude that the receptor-binding activity of bacterially synthesized met-hGH and pituitary hGH are identical, suggesting a common tertiary structure.

Original languageEnglish (US)
Pages (from-to)202-209
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume106
Issue number1
DOIs
StatePublished - May 14 1982

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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