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PMID: 47888 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Isolation and analysis of the mechanism of action of an inactivator of C4b in normal human serum.

The Journal of experimental medicine ·Vol. 141 ·No. 4 ·1975-04-01 ·Pages 890-903

Cooper NR

Abstract

A complement regulatory principle, C4b inactivator, was isolated in a partially purified form from normal human serum. The C4b inactivator, a beta1-globulin with an approximate mol wt of 88,000 daltons, and which may be identical to C3b inactivator, cleaved C4b in free solution or on the surface of cells and rendered it unable to participate in hemolytic reactions or to interact with cells, having receptors for C4b. C/b inactivator functioned by cleaving the alpha-polypeptide chain of C4b at a single site which was sufficient to dissociate the molecule into two fragments, C4c and C4d, and to inactivate it biological function. Certain structural correlates of C4 functions deriving from these studies are discussed and a model for C4 structure based on these findings is presented.

MeSH Terms
Animals Antigen-Antibody Reactions Beta-Globulins Blood Protein Electrophoresis Blood Proteins/isolation & purification Cattle/immunology Chromatography Complement Inactivator Proteins Electrophoresis, Disc Epitopes Erythrocytes/immunology Hemolysis Immune Adherence Reaction Immunochemistry Immunoelectrophoresis Iodine Radioisotopes Protein Binding Sodium Dodecyl Sulfate Ultracentrifugation
Chemicals
Beta-Globulins Blood Proteins Complement Inactivator Proteins Epitopes Iodine Radioisotopes Sodium Dodecyl Sulfate
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Cooper N R
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26 references, click to expand
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Article Info
Journal
The Journal of experimental medicine
Abbr.
J Exp Med
ISSN
0022-1007
Published
1975-04-01
Pages
890-903
Language
English
Region
United States
NLM ID
2985109R
PMCID
PMC2189755
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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