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International journal of peptide and protein research1987; 29(5); 589-595; doi: 10.1111/j.1399-3011.1987.tb02288.x

Conformation of equine pituitary somatotropin.

Abstract: Equine pituitary somatotropin (growth hormone) has been studied by zero-order and second-order absorption spectroscopy, and by circular dichroism. Difference absorption spectra have also been generated during proteolytic digestion of the hormone. The molar extinction coefficient of the native protein was found to be 16,050 +/- 330 M-1 cm-1 at 278.1 nm. Comparison of the conformations of equine somatotropin and somatotropins isolated from several other mammalian species indicates a close structural relationship between these molecules. With the increasing number of species which have been studied, it is becoming evident that with regard to conformation, the somatotropins can be subdivided into at least three major groups.
Publication Date: 1987-05-01 PubMed ID: 3610473DOI: 10.1111/j.1399-3011.1987.tb02288.xGoogle Scholar: Lookup
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  • Journal Article
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

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This study investigated the structure of the equine pituitary somatotropin, also known as the growth hormone, in horses using various spectroscopy techniques. The results revealed significant structural similarities between this hormone in horses and other mammals, lending further weight to the idea that somatotropins can be grouped into at least three major categories based on their structure.

Research Methods and Procedures

  • The researchers used both zero-order and second-order absorption spectroscopy to study the growth hormone. These are techniques used to examine how a substance absorbs light at different wavelengths, which can provide information about the substance’s structure and composition.
  • Circular dichroism, another analytical method that can give insights into a substance’s structure, was also deployed.
  • By generating difference absorption spectra during the proteolytic digestion of the hormone, the researchers were able to study the changes that occur in the protein structure during this process.

Findings of the Research

  • The molar extinction coefficient of the native protein was established to be 16,050 +/- 330 M-1 cm-1 at 278.1 nm. This coefficient is a measure of how strongly the protein absorbs light at a particular wavelength, which can provide insights into its structure.
  • Notably, the research revealed a close structural relationship between the growth hormone in horses and that in numerous other mammalian species.
  • This finding supports the growing belief that somatotropins, based on their structure, can be subdivided into at least three major groups. A similar structure may suggest a similar function, underscoring the shared elements in growth processes across different species.

Implications of the Study

  • This research makes notable contributions to our understanding of the hormone somatotropin in horses and other mammals. The information can be useful in studies focusing on the hormonal regulation of growth and development in these animals.
  • Moreover, the research methodologies used in this study can serve as a model for future research into protein structure and function in other species, thereby driving advancements in the field of endocrinology.
  • Finally, understanding the similarities and differences in hormone structures across various species may help develop targeted treatments for growth disorders.

Cite This Article

APA
Bewley TA, Li CH. (1987). Conformation of equine pituitary somatotropin. Int J Pept Protein Res, 29(5), 589-595. https://doi.org/10.1111/j.1399-3011.1987.tb02288.x

Publication

ISSN: 0367-8377
NlmUniqueID: 0330420
Country: Denmark
Language: English
Volume: 29
Issue: 5
Pages: 589-595

Researcher Affiliations

Bewley, T A
    Li, C H

      MeSH Terms

      • Animals
      • Circular Dichroism
      • Growth Hormone
      • Horses
      • Peptide Fragments
      • Protein Conformation
      • Spectrophotometry, Ultraviolet
      • Thermolysin
      • Trypsin

      Grant Funding

      • AM-18677 / NIADDK NIH HHS
      • AM-6097 / NIADDK NIH HHS

      Citations

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