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Archives of biochemistry and biophysics1983; 227(2); 618-625; doi: 10.1016/0003-9861(83)90491-5

Studies on prolactin: conformational comparison of human, equine, and porcine pituitary prolactins.

Abstract: The conformations of human, equine, and porcine pituitary prolactins, as evidenced by various optical properties, have been compared. The alpha-helix contents of all three proteins are essentially identical to each other (60 +/- 5%), as well as to prolactins isolated from other mammalian species. Direct absorption (zero and second-order), difference absorption, fluorescence emission, and circular dichroism spectra suggest that the majority of tyrosine and tryptophan side chains in these three proteins exist in very similar microenvironments within the folded forms of the hormones. Thus, the general conformational properties of these molecules are closely related to each other, and to other mammalian prolactins. Molar extinction and absorptivity values have been obtained at the absorption maximum of each species. In addition, a second molar extinction value has been determined at a particular wavelength found to be different for each, and which appears to be independent of the conformational state of the molecule. These absorptivities are useful in providing accurate prolactin concentrations in the 10(0) to 10(-2) mg/ml range. On incubation with the proteolytic enzyme thermolysin, all three hormones display an initial, short lag period during which little conformational change can be detected by difference absorption spectroscopy. For human and porcine prolactins, subsequent rates of proteolytically induced conformational collapse were found to be essentially identical. However, under similar conditions, equine prolactin loses its conformation significantly more slowly.
Publication Date: 1983-12-01 PubMed ID: 6667032DOI: 10.1016/0003-9861(83)90491-5Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

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The research compares the structure and properties of the hormone prolactin in humans, horses, and pigs, revealing their high similarity across these species. Prolactin concentration measures are provided, aiding accuracy in biological and medical research.

Research Overview

  • The study focuses on comparing the conformations or structures of the hormone prolactin in humans, horses, and pigs.
  • The researchers utilized several optical properties like direct absorption, fluorescence emission, and circular dichroism spectra to gather evidence of the similarities and differences in these hormones.

Similarities in Prolactin Across Species

  • The research found that the alpha-helix content, a specific structural element in proteins, of prolactins in all three species was roughly the same (60 ± 5%).
  • The side chains of two of the amino acids that make up these proteins, tyrosine and tryptophan, were found to exist in similar microenvironments within the folded forms of the hormones in these species.
  • These findings suggest that the general conformations or structures of prolactins in different species are closely related to each other.

Measuring Prolactin Concentration

  • Molar extinction and absorptivity values were obtained at the absorption maximum of each species, which helped in determining accurate prolactin concentrations ranging from 10(0) to 10(-2) mg/ml.
  • A second molar extinction value was determined at a unique wavelength for each species, independent of the conformational state of the molecule.

Prolactin Reaction to Proteolytic Enzyme Thermolysin

  • When the three types of prolactin hormones were incubated with the protease thermolysin, the proteins underwent an initial short lag period during which little change in their conformation could be observed.
  • However, the speed at which the proteins then collapsed, under the action of thermolysin, varied across species. While the prolactin from humans and pigs displayed similar rates of collapse, the horse prolactin’s structure decayed more slowly under the same conditions.

Cite This Article

APA
Bewley TA, Li CH. (1983). Studies on prolactin: conformational comparison of human, equine, and porcine pituitary prolactins. Arch Biochem Biophys, 227(2), 618-625. https://doi.org/10.1016/0003-9861(83)90491-5

Publication

ISSN: 0003-9861
NlmUniqueID: 0372430
Country: United States
Language: English
Volume: 227
Issue: 2
Pages: 618-625

Researcher Affiliations

Bewley, T A
    Li, C H

      MeSH Terms

      • Animals
      • Chemical Phenomena
      • Chemistry
      • Disulfides / isolation & purification
      • Horses
      • Humans
      • Pituitary Gland / analysis
      • Prolactin / isolation & purification
      • Protein Conformation
      • Species Specificity
      • Spectrophotometry
      • Swine

      Grant Funding

      • AM-6097 / NIADDK NIH HHS

      Citations

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