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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Veröffentlicht in:	Biochemistry and molecular biology international 1996-10, Vol.40 (3), p.433-446
Hauptverfasser:	Schauenstein, Erwin, Schauenstein, Konrad, Dachs, Franz, Reiter, Monika, Leitsberger, Astrid, Weblacher, Michaela, Maninger, Karin, Horejsi, Helene, Steinschifter, Waltraud, Hirschmann, Carola, Felsner, Peter
Format:	Artikel
Sprache:	eng
Schlagworte:	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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Zusammenfassung:	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