| Autor: |
B. Whitaker, Marian Kruszynski, R. E. Jordan, D. De Riggi, A. Schmidt, G. A. Heavner |
| Rok vydání: |
2009 |
| Předmět: |
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| Zdroj: |
Advances in Experimental Medicine and Biology ISBN: 9780387736563 |
| DOI: |
10.1007/978-0-387-73657-0_177 |
| Popis: |
Introduction There are naturally occurring human antibodies to the F(ab’)2 portion of IgG [1]. Extracellular proteases and bacterial enzymes can cleave the IgG hinge region and release the Fc domain (with its effector functions. The human immune repertoire contains auto-antibodies that are directed against endogenous Fab and F(ab’)2 fragments [2]. The anti-fragment reactivity is at newly exposed epitopes in the cleaved IgG hinge region. By systematically constructing a bi-directional approach of 14-mer biotinylated peptides through the hinge region with either a free C-termini or free N-termini for each position of the hinge, one can study other single heavy chain terminal positions (eg. Fab, F(ab’)2 and Fc) at which no proteases that cleave IgG have been identified. By exposing streptavidin-captured peptides to human serum, immune reactivity could be identified at various free carboxy termini sites. This mapping approach will aid in identifying pre-existing auto-antibodies that recognize the newly-generated epitopes which correspond to protease cleavage sites in IgG and possibly to other non-IgG proteins. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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