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Related Experiment Videos

Copper(II)-binding ability of human alpha-fetoprotein

Y Aoyagi, T Ikenaka, F Ichida

    Cancer Research
    |October 1, 1978
    PubMed
    Summary

    Human alpha-fetoprotein binds copper(II) ions, similar to albumin. This binding is primarily mediated by a histidyl residue in the protein's amino-terminal region.

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    Area of Science:

    • Biochemistry
    • Proteomics

    Background:

    • Human alpha-fetoprotein (AFP) is a major serum protein.
    • AFP's role in copper transport and its binding characteristics are not fully understood.

    Purpose of the Study:

    • To investigate the copper(II)-binding properties of human alpha-fetoprotein.
    • To identify the specific residues involved in copper(II) binding.

    Main Methods:

    • Purification of AFP from umbilical cord serum and hepatoma ascites fluid.
    • Equilibrium dialysis and gel filtration assays to determine binding capacity.
    • Photooxidation studies to assess the role of histidine residues.

    Main Results:

    • AFP exhibits pH-dependent copper(II) binding, similar to albumin.
    • AFP binds 1 mol of copper(II) per mol of protein above pH 6.0.
    • Binding capacity decreased at pH 5.4, correlating with histidine imidazole pK.
    • Photooxidation destroyed copper(II)-binding ability and histidyl residues.
    • A synthetic amino-terminal peptide of AFP also bound copper(II).

    Conclusions:

    • The histidyl residue in the amino-terminal region is crucial for AFP's copper(II)-binding ability.
    • These findings elucidate a key functional aspect of alpha-fetoprotein in copper homeostasis.

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