[Description of an unusual enzymic activity cleaving the third component of complement].
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A large enzymatic complex cleaving C3 (C3'ase) in the absence of magnesium (EDTA) has been partially characterized in two patients. On gel filtration EDTA-C3'ase was found in an 800 000 fraction containing antigenic C4, IgA and IgG in addition to alpha-2-macroglobulin and IgM normally present. EDTA-C3'ase was specifically neutralized by antibodies to IgG, IgA and C4. The characteristics of this unusual enzymatic complex are compatible with that of a C4b2a complex stabilized by its specific binding to an auto-antibody of the IgG and/or IgA class.
Molecular Weight, Hot Temperature, Drug Stability, Complement Activating Enzymes, Multienzyme Complexes, Chromatography, Gel, Humans, Complement C3-C5 Convertases, Edetic Acid, Substrate Specificity
Molecular Weight, Hot Temperature, Drug Stability, Complement Activating Enzymes, Multienzyme Complexes, Chromatography, Gel, Humans, Complement C3-C5 Convertases, Edetic Acid, Substrate Specificity
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