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Elephant growth hormone. Isolation and characterization.

C H Li, T A Bewley, D Chung

    International Journal of Peptide and Protein Research
    |January 1, 1987
    PubMed
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    Researchers purified elephant growth hormone, revealing its structure and lower somatotropin activity compared to bovine growth hormone. Structural analysis suggests a unique hydrogen bond involving its single tryptophan residue.

    Area of Science:

    • Biochemistry
    • Endocrinology
    • Structural Biology

    Background:

    • Growth hormone (GH) is crucial for growth and metabolism.
    • Understanding GH from diverse species aids comparative endocrinology.
    • Elephant GH structure and function remain largely uncharacterized.

    Purpose of the Study:

    • To purify and characterize elephant growth hormone (eGH).
    • To determine the structural features and somatotropin activity of eGH.

    Main Methods:

    • Purification of eGH from pituitary glands.
    • Amino acid composition analysis.
    • Radioreceptor binding assay for somatotropin activity.
    • Circular dichroism (CD) spectroscopy for secondary structure estimation.

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  • Difference absorption spectroscopy for tryptophan environment analysis.

    • Main Results:

    • Homogeneous eGH purified, comprising 191 amino acids.
    • eGH exhibits 15% somatotropin activity compared to bovine GH in radioreceptor assays.
    • CD spectra indicate approximately 50% alpha-helical content.
    • Difference absorption spectra suggest a hydrogen bond between the single tryptophan residue and a carboxylate ion.

    Conclusions:

    • Elephant growth hormone possesses distinct structural and functional characteristics.
    • The reduced activity may be linked to its specific structural features.
    • Further studies are warranted to elucidate the precise role of eGH in elephant physiology.