Reactive disulfide bonds in immunoglobulin G. A unique feature in serum proteins of different species

A reactive disulfide bond (SS)* was detected and characterized in IgG of humans, rats and mice by virtue of disulfide interchange with dithionitrobenzoate. (SS)* was found exclusively in human IgG1 and rat IgG2b. In human IgG1 (SS)* was identified as the upper one of the two interheavy bridges in th...

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Bibliographic Details
Published in:Biochemistry and molecular biology international 1996-10, Vol.40 (3), p.433-446
Main Authors: Schauenstein, Erwin, Schauenstein, Konrad, Dachs, Franz, Reiter, Monika, Leitsberger, Astrid, Weblacher, Michaela, Maninger, Karin, Horejsi, Helene, Steinschifter, Waltraud, Hirschmann, Carola, Felsner, Peter
Format: Article
Language:English
Subjects:
Animals
Autoradiography
Blood Proteins - chemistry
Blood Proteins - metabolism
Carbon Radioisotopes
complement activation
disulfide interchange
Disulfides - chemistry
Disulfides - metabolism
dithionitrobenzoate
Dithionitrobenzoic Acid - chemistry
Free Radicals
Humans
Immunoglobulin G - chemistry
Immunoglobulin G - metabolism
Immunoglobulins G
Kinetics
Mice
Rats
Rats, Sprague-Dawley
reactive interheavy S‐S bonds
Sulfhydryl Compounds
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Summary:A reactive disulfide bond (SS)* was detected and characterized in IgG of humans, rats and mice by virtue of disulfide interchange with dithionitrobenzoate. (SS)* was found exclusively in human IgG1 and rat IgG2b. In human IgG1 (SS)* was identified as the upper one of the two interheavy bridges in the hinge, where it appears to take part in complement activation. The biological significance of (SS)* in IgG was underlined by the fact that no other serum proteins were found to exhibit a similar reactivity.
ISSN:1521-6543
1039-9712
1521-6551
DOI:10.1080/15216549600201003