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A glycosylated prolactin species is covalently bound to immunoglobulin in human amniotic fluid

L J Heffner1, L S Gramates, R W Yuan

  • 1Department of Obstetrics, Gynecology and Reproductive Biology, Brigham and Women's Hospital, Boston, MA.

Biochemical and Biophysical Research Communications
|November 30, 1989
PubMed

Insights

Glycosylated prolactin in amniotic fluid is covalently bound to another protein. Further analysis shows this protein is immunoglobulin, linked via disulfide bonds, impacting prolactin function.

Area of Science:

  • Biochemistry
  • Reproductive Biology
  • Immunology

Background:

  • Prolactin is a key hormone in reproduction and lactation.
  • Glycosylation of prolactin can alter its biological activity.
  • Amniotic fluid contains various proteins, including hormones and immunoglobulins.

Purpose of the Study:

  • To investigate the molecular form of glycosylated prolactin in amniotic fluid.
  • To identify proteins covalently bound to glycosylated prolactin.
  • To elucidate the nature of the linkage between glycosylated prolactin and other proteins.

Main Methods:

  • Western immunoblotting for protein separation and detection.
  • High-performance liquid chromatography (HPLC) for purification.
  • Protein isolation techniques to identify binding partners.

Main Results:

  • Western blots indicated glycosylated prolactin is covalently bound to another protein.
  • Demonstrated that a specific glycosylated prolactin species is linked to immunoglobulin.
  • Identified disulfide bonds as the mediating linkage in amniotic fluid.

Conclusions:

  • A novel form of prolactin exists in amniotic fluid, bound to immunoglobulin.
  • Disulfide bond linkage suggests a specific post-translational modification or interaction.
  • Understanding this interaction is crucial for comprehending prolactin's role in the amniotic environment.

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