Abstract
A method has been described for the chemical modification of human C'2 which results in a pronounced enhancement of its hemolytic activity and a marked increase in the stability of the intermediate complex EAC'1a,4,2a prepared with the modified C'2. Both effects are fully explained by the observed increase in activity and stability of the C'3 converting enzyme, C'4,2a, following its generation with modified C'2. Evidence has been presented in support of the hypothesis that the modification resulting from treatment of C'2 with a critical concentration of iodine consists of oxidation of one or more sulfhydryl group within the molecule.
MeSH Terms
Animals
Biological Assay
Complement System Proteins/analysis,physiology
Cysteine/pharmacology
Edetic Acid/pharmacology
Esterases/analysis
Glutathione/pharmacology
Hemolysis/drug effects
Humans
Immunochemistry
In Vitro Techniques
Iodine/pharmacology
Iodoacetates/pharmacology
Mercaptoethanol/pharmacology
Oxidation-Reduction
Rabbits
Sheep
Sulfhydryl Compounds/pharmacology
Chemicals
Iodoacetates
Sulfhydryl Compounds
Mercaptoethanol
Complement System Proteins
Iodine
Edetic Acid
Esterases
Glutathione
Cysteine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Polley M J
Müller-Eberhard H J
References (14)
14 references, click to expand
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