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Related Experiment Videos

Mouse C3b/C4b inactivator: purification and properties.

S Kai, T Fujita, I Gigli

    Journal of Immunology (Baltimore, Md. : 1950)
    |December 1, 1980
    PubMed
    Summary
    This summary is machine-generated.

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    Mouse C3b/C4b inactivator (C3b/C4bINA) is a beta-globulin that cleaves C4b and C3b proteins. This study characterizes its structure, function, and interaction with other complement proteins.

    Area of Science:

    • Biochemistry
    • Immunology
    • Complement System

    Background:

    • Mouse C3b/C4b inactivator (C3b/C4bINA) is a key regulator of the complement system.
    • Understanding its function is crucial for comprehending immune responses and potential therapeutic targets.

    Purpose of the Study:

    • To purify and characterize mouse C3b/C4bINA.
    • To investigate its enzymatic activity on complement components C4b and C3b.
    • To explore its interactions with C4-binding protein (C4-bp) and beta 1H.

    Main Methods:

    • Purification of mouse C3b/C4bINA from mouse serum.
    • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to determine molecular weight.
    • Enzymatic assays to assess cleavage of C4b and C3b.

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  • Crossed immunoelectrophoresis to identify related proteins.

    • Main Results:

    • Mouse C3b/C4bINA was purified and found to be a beta-globulin composed of two disulfide-bonded chains (60,000 and 35,000 m.w.).
    • It cleaves cell-bound C4b and fluid-phase C4b (in the presence of C4-bp).
    • It also cleaves human C3b in solution (with human beta 1H), suggesting homology with human C3b/C4bINA.
    • An inactive, antigenically identical precursor protein was detected.

    Conclusions:

    • Mouse C3b/C4bINA is a multifunctional complement regulator with distinct cleavage activities on C4b and C3b.
    • Its function is modulated by accessory proteins like C4-bp and beta 1H.
    • The identification of an inactive precursor suggests a regulatory mechanism for C3b/C4bINA activity.