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Selected Publication:
Schauenstein, E; Schauenstein, K; Dachs, F; Reiter, M; Leitsberger, A; Weblacher, M; Maninger, K; Horejsi, H; Steinschifter, W; Hirschmann, C; Felsner, P.
Reactive disulfide bonds in immunoglobulin G. A unique feature in serum proteins of different species.
Biochem Mol Biol Int. 1996; 40(3):433-446
Doi: 10.1080/15216549600201003
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- Co-authors Med Uni Graz
- Horejsi Renate
- Schauenstein Konrad
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- Abstract:
- 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.
- Find related publications in this database (using NLM MeSH Indexing)
- Animals -
- Autoradiography -
- Blood Proteins - chemistry
- Carbon Radioisotopes - chemistry
- Disulfides - chemistry
- Dithionitrobenzoic Acid - chemistry
- Free Radicals - chemistry
- Humans - chemistry
- Immunoglobulin G - chemistry
- Kinetics - chemistry
- Mice - chemistry
- Rats - chemistry
- Rats, Sprague-Dawley - chemistry
- Sulfhydryl Compounds - chemistry
- Find related publications in this database (Keywords)
- Immunoglobulins G
- Reactive Interheavy S-S Bonds
- Disulfide Interchange
- Dithionitrobenzoate
- Complement Activation