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Primary structure of human alpha 2-macroglobulin. V. The complete structure.

L Sottrup-Jensen, T M Stepanik, T Kristensen

    The Journal of Biological Chemistry
    |July 10, 1984
    PubMed
    Summary

    The primary structure of human alpha 2-macroglobulin, a tetrameric glycoprotein, was determined, revealing its 1451 amino acid subunits and key reactive sites. This study also suggests evolutionary links between alpha 2-macroglobulin and complement components C3 and C4.

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    Area of Science:

    • Biochemistry
    • Proteomics
    • Structural Biology

    Background:

    • Human alpha 2-macroglobulin is a tetrameric plasma glycoprotein with crucial roles in regulating proteolytic systems.
    • Understanding its primary structure is essential for elucidating its function and interactions.

    Purpose of the Study:

    • To determine the complete primary structure of human alpha 2-macroglobulin.
    • To identify key structural features, including amino acid sequence, glycosylation sites, disulfide bridges, and reactive centers.
    • To explore potential evolutionary relationships with other related proteins.

    Main Methods:

    • Amino acid sequencing of the 1451-residue subunits.
    • Identification of asparagine-linked oligosaccharide attachment sites.
    • Mapping of eleven intrachain and one probable interchain disulfide bridges.

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  • Characterization of the thiol ester bond and potential transglutaminase cross-linking sites.

    • Main Results:

    • The complete amino acid sequence of the alpha 2-macroglobulin subunit (1451 residues) was established.
    • Specific sites for glycosylation, disulfide bonding, and covalent complex formation were identified.
    • The molecular weight of the subunit was determined to be 160,837 (unmodified) and approximately 179,000 (glycosylated).
    • Sequence comparisons revealed evolutionary relationships between alpha 2-macroglobulin and complement components C3 and C4.

    Conclusions:

    • The determined primary structure provides a foundation for understanding alpha 2-macroglobulin's function in protease regulation.
    • The identified reactive sites are critical for its mechanism of action.
    • Alpha 2-macroglobulin and complement proteins C3/C4 share evolutionary origins, highlighting conserved biological functions.