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Related Experiment Videos

Glycosylated human prolactin.

U J Lewis, R N Singh, Y N Sinha

    Endocrinology
    |January 1, 1985
    PubMed
    Summary

    Researchers isolated a glycosylated form of human prolactin (G-hPRL) from pituitary glands. This glycoprotein differs in molecular weight and RIA reactivity from the major prolactin form.

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    Area of Science:

    • Endocrinology
    • Glycobiology
    • Protein Chemistry

    Background:

    • Human prolactin (hPRL) is a key hormone involved in numerous physiological processes.
    • Post-translational modifications, such as glycosylation, can alter protein function and characteristics.
    • Understanding different forms of hPRL is crucial for accurate physiological and diagnostic assessments.

    Purpose of the Study:

    • To isolate and characterize a glycosylated form of human prolactin (G-hPRL).
    • To determine the properties and potential site of glycosylation of G-hPRL.
    • To compare the immunoreactivity of G-hPRL with the major form of hPRL.

    Main Methods:

    • Isolation of G-hPRL from pituitary glands using lentil lectin-Sepharose 4B chromatography.
    • Elution of bound glycoprotein with methyl-alpha-D-mannopyranoside.
    • Molecular weight determination by SDS-gel electrophoresis.
    • Radioimmunoassay (RIA) to assess immunoreactivity compared to the principal hPRL form.

    Main Results:

    • A distinct glycosylated form of human prolactin (G-hPRL) was successfully separated from the major hPRL form.
    • G-hPRL exhibited a higher molecular weight (25,000 Da) compared to the principal hPRL (23,000 Da).
    • G-hPRL showed approximately one-third the immunoreactivity of the principal hPRL in RIA assays.

    Conclusions:

    • The identified G-hPRL represents a unique post-translational modification of human prolactin.
    • The glycosylation likely occurs at the asparagine residue at position 31, the sole Asn-X-Ser(Thr) site in hPRL.
    • The altered molecular weight and reduced immunoreactivity of G-hPRL have implications for its biological activity and detection.

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