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Related Experiment Videos

Human placenta beta-galactoside-binding lectin. Purification and some properties.

J Hirabayashi, K Kasai

    Biochemical and Biophysical Research Communications
    |August 16, 1984
    PubMed
    Summary

    Researchers isolated a beta-galactoside-binding lectin from human placenta. This protein, similar to other vertebrate lectins, was purified using affinity chromatography and characterized by its molecular weight and isoelectric point.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Background:

    • Beta-galactoside-binding lectins are proteins involved in cell recognition and adhesion.
    • These lectins play roles in various biological processes, including development and immunity.
    • Human placenta is a rich source of various proteins, including lectins.

    Purpose of the Study:

    • To isolate and characterize a novel beta-galactoside-binding lectin from human placenta.
    • To determine the biochemical properties of the purified lectin.
    • To compare the lectin with other known vertebrate beta-galactoside-binding lectins.

    Main Methods:

    • Extraction of lectin from human placenta homogenate using a lactose solution.
    • Purification of the lectin to apparent homogeneity via affinity chromatography on asialofetuin-Sepharose.

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  • Determination of subunit molecular weight and isoelectric point.

    • Main Results:

    • A beta-galactoside-binding lectin was successfully isolated and purified.
    • The lectin exhibited an apparent subunit molecular weight of 13,800 and an isoelectric point of approximately 5.
    • Hemagglutinating activity was inhibited by D-galactose-containing saccharides.
    • The purified lectin shared biochemical characteristics with other vertebrate beta-galactoside-binding lectins.

    Conclusions:

    • A novel beta-galactoside-binding lectin was identified in human placenta.
    • The lectin's properties suggest its involvement in galactose-dependent biological interactions.
    • This finding contributes to the understanding of lectin diversity and function in vertebrates.