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Updated: Aug 2, 2026
Measuring the 50% Haemolytic Complement (CH50) Activity of Serum
Published on: March 29, 2010
Chromatographic resolution of the first component of human complement into three activities
Insights
Human complement component 1 (C
Area of Science:
- Immunology
- Biochemistry
- Complement System
Background:
- The human complement system is a crucial part of innate immunity.
- Complement component 1 (C'1) is the first component activated in the classical pathway.
- Understanding C'1's structure and function is vital for deciphering complement-mediated immune responses.
Purpose of the Study:
- To chromatographically resolve the human C'1 euglobulin fraction.
- To identify and characterize the individual components of C'1.
- To elucidate the roles of C'1 components in hemolytic reactions and C'1 esterase generation.
Main Methods:
- Chromatographic resolution of human C'1 euglobulin fraction using DEAE cellulose.
- Assay of hemolytic activities of isolated C'1 components.
- Characterization of C'1 components based on their functional properties and sedimentation behavior.
Main Results:
- C'1 was resolved into three distinct activities: C'1q, C'1r, and C'1s.
- C'1q was identified as the previously known 11S component involved in early complement activation.
- C'1r was identified as a novel complement component, and C'1s was identified as C'1 proesterase.
Conclusions:
- The three components C'1q, C'1r, and C'1s are essential for C'1 esterase generation.
- C'1 esterase plays a central role in complement activation involving C'1, C'4, and C'2.
- This study provides a detailed characterization of C'1 components and their functional significance in the complement cascade.
Abstract:
A euglobulin fraction of human C'1 has been chromatographically resolved into three distinct activities, designated C'1q, C'1r, and C'1s, in the order of their elution from DEAE cellulose. All three of these activities have been shown to participate in various hemolytic reactions requiring C'1, including the cold phase of the Donath-Landsteiner reaction, and to be necessary for generation of C'1 esterase. C'1q was identical with a previously described serum protein implicated in a very early step of complement action and designated the 11S component on the basis of its sedimentation constant. C'1r could not be related to a known complement activity and has been presented as a new component. C'1s, on the basis of chromatographic evidence, was identified with C'1 proesterase. Methods of assay of these components of C'1 have been presented. The significance of C'1q, C'1r, and C'1s in generation of C'1 esterase and the central role of this enzyme in reactions involving C'1, C'4, and C'2 have been discussed.
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