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Related Experiment Videos

Characterization of electrophoretically separable endorphins in human CSF.

F Nyberg, A Wahlström, B Sjölund

    Brain Research
    |January 24, 1983
    PubMed
    Summary

    Researchers purified opioid peptides from human cerebrospinal fluid, identifying Met-enkephalin-Lys6 and dynorphin-like structures. These novel opioid peptides are present at higher concentrations than previously known endorphins.

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    Area of Science:

    • Neuroscience
    • Biochemistry
    • Pharmacology

    Background:

    • Opioid peptides modulate pain and mood.
    • Human cerebrospinal fluid (CSF) is a source of endogenous opioid peptides.
    • Previous studies identified enkephalins and endorphins in CSF.

    Purpose of the Study:

    • To purify and characterize opioid peptides from human CSF.
    • To identify novel opioid peptide structures in human CSF.
    • To quantify the relative concentrations of identified opioid peptides.

    Main Methods:

    • Large-scale purification of human CSF using Sephadex G-10 chromatography and agarose electrophoresis.
    • Characterization of purified fractions using High-Performance Liquid Chromatography (HPLC) and radioimmunoassay.

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  • Guidance of all purification steps by a radioreceptor assay.

    • Main Results:

    • Two main fractions with receptor activity were isolated: Fraction I (FI) and Fraction II (FII).
    • Fraction FIIA was identified as Met-enkephalin-Lys6, and a basic FI component showed similarity to dynorphin.
    • These identified opioid peptides were found at higher concentrations than Met-enkephalin, Leu-enkephalin, dynorphin, or beta-endorphin.

    Conclusions:

    • Human CSF contains previously unidentified opioid peptide structures.
    • Met-enkephalin-Lys6 and dynorphin-like peptides are significant endogenous opioid components in human CSF.
    • The higher concentrations suggest these peptides play a crucial role in central nervous system functions.