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Aggregation of binding protein from rat nerve

D M Peach, J C Russell

    Physiological Chemistry and Physics
    |January 1, 1978
    PubMed
    Summary
    This summary is machine-generated.

    Leucine-binding protein forms large, dynamic polymers influenced by colchicine and magnesium ions. This adaptable protein complex exhibits Mg2+-ATPase activity, suggesting responsiveness to environmental conditions.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Protein Dynamics

    Background:

    • Previous research identified a leucine-binding protein.
    • The dynamic properties of this protein system required further characterization.

    Purpose of the Study:

    • To investigate the dynamic properties and polymerization of leucine-binding protein.
    • To understand the factors influencing its complex formation and enzymatic activity.

    Main Methods:

    • Analysis of protein polymerization under varying conditions (colchicine, Mg2+).
    • Enzymatic digestion assays using trypsin, RNAase, and collagenase.
    • Assay for Mg2+-ATPase activity in the polymer fraction.

    Main Results:

    • Leucine-binding protein self-assembles into a large polymer/complex (>302,000 daltons).

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  • Colchicine inhibits polymerization, while Mg2+ promotes it.
  • The polymer is sensitive to trypsin but resistant to RNAase and collagenase.
  • Mg2+-ATPase activity was detected in the polymer fraction.

    • Conclusions:

    • Leucine-binding protein forms a large, dynamic complex.
    • Polymerization is modulated by specific ions and molecules.
    • The complex possesses Mg2+-ATPase activity, indicating functional adaptability.
    • The structure is adaptable to ionic and environmental changes.