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Related Experiment Videos

Conformational changes of complement components C3 and B induced at higher temperature.

A Takada, S Shirahama, Y Takada

    Complement (Basel, Switzerland)
    |January 1, 1985
    PubMed
    Summary
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    The human complement proteins C3 and B undergo significant conformational changes at low temperatures, impacting their function and interaction within the complement system.

    Area of Science:

    • Immunology
    • Biochemistry
    • Complement System

    Background:

    • The human complement system is crucial for innate and adaptive immunity.
    • Complement proteins C3 and B play vital roles in complement activation pathways.
    • Understanding the thermal stability and conformational changes of these proteins is essential for comprehending their function.

    Purpose of the Study:

    • To investigate the thermal denaturation and conformational changes of human complement proteins C3 and B.
    • To determine the effect of temperature on the functional activity and structural integrity of C3 and B.
    • To elucidate the relationship between conformational alterations and the catalytic activity of complement components.

    Main Methods:

    • Incubation of purified human complement C3 and B at various temperatures.

    Related Experiment Videos

  • Assay of antibody combining capability and C3 conversion.
  • Spectroscopic analysis using 1-anilino-8-naphthalene sulfonate (ANS) to detect hydrophobicity changes.
  • Monitoring fluorescence intensity changes of C3.

    • Main Results:

    • Complement protein B lost antibody combining capability at 46°C, while C3 lost it above 50°C.
    • C3 conversion was significantly reduced in the presence of heated B (44-46°C) and abolished at 50°C.
    • Thermal denaturation led to increased surface hydrophobicity in both C3 and B, indicating conformational shifts.

    Conclusions:

    • Human complement proteins C3 and B exhibit low melting points, undergoing drastic conformational changes at relatively low temperatures.
    • These temperature-induced conformational alterations significantly impact the functional activities of C3 and B within the complement cascade.
    • The findings provide insights into the structural dynamics of complement proteins and their susceptibility to thermal stress.