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. 1982 Apr 1;203(1):293-8.
doi: 10.1042/bj2030293.

Purification of human C3b inactivator by monoclonal-antibody affinity chromatography

L Hsiung, A N Barclay, M R Brandon, E Sim, R R Porter

Purification of human C3b inactivator by monoclonal-antibody affinity chromatography

L Hsiung et al. Biochem J. .

Abstract

Monoclonal antibody has been obtained to the human complement control protein C3b inactivator after immunization of mice with the enzyme prepared by conventional methods. Antibody from ascitic fluid was purified and coupled to Sepharose-CL-4B to give a specific affinity column, which was used to isolate C3b inactivator from human serum in 70% yield. The product was characterized by size, chain structure, amino acid analysis and proteolytic activity.

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References

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