Related Experiment Video
Updated: Jun 19, 2026

08:26
Measuring the 50% Haemolytic Complement (CH50) Activity of Serum
Published on: March 29, 2010
THE PREPARATION AND PHYSICOCHEMICAL CHARACTERIZATION OF THE SERUM PROTEIN COMPONENTS OF COMPLEMENT
L Pillemer1, E E Ecker, J L Oncley
1Department of Physical Chemistry, Harvard Medical School, Boston, and the Institute of Pathology, Western Reserve University, and the University Hospitals, Cleveland.
The Journal of Experimental Medicine
|October 30, 2009
Summary
Researchers purified three complement components from guinea pig serum: mid-piece, end-piece, and the 4th component. This study details their separation methods and biochemical properties for further immunological research.
Area of Science:
- Immunology
- Biochemistry
Background:
- Complement system components are crucial for immune responses.
- Purification of individual complement factors is essential for understanding their specific functions.
Purpose of the Study:
- To describe methods for isolating and purifying three complement components from guinea pig serum.
- To characterize the biochemical properties of these purified components.
Main Methods:
- Separation of complement components using biochemical techniques.
- Characterization of purified components via electrophoresis and sedimentation analysis.
Main Results:
- Mid-piece was isolated as a euglobulin with specific electrophoretic mobility and sedimentation constant.
- End-piece and 4th component were co-purified in a euglobulin fraction containing carbohydrates.
Conclusions:
- Successful purification of key complement components from guinea pig serum was achieved.
- The study provides foundational data on the biophysical properties of mid-piece, end-piece, and the 4th component.
Related Concept Videos
Complement System
The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a membrane...
Immunoprecipitation
Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...
