Proceedings: X-ray diffraction analysis of immunoglobulin structure.

R Huber; J Deisenhofer; P M Colman; O Epp; H Fehlhammer; W Palm

Home/Archive/PubMed

PubMed · 964922

Proceedings: X-ray diffraction analysis of immunoglobulin structure.

R Huber·J Deisenhofer·P M Colman·O Epp·H Fehlhammer·W Palm

View original source ↗Export metadata ↓

Abstract

The source did not provide an abstract. Follow the original record for more information.

Explore related subjects

Immunoglobulin Fc Fragments Immunoglobulin G Protein Conformation X-Ray Diffraction Journal Article

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

R Huber, J Deisenhofer, P M Colman, O Epp, H Fehlhammer, W Palm. 1976. Proceedings: X-ray diffraction analysis of immunoglobulin structure.. https://pubmed.ncbi.nlm.nih.gov/964922/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed1995

The enhancement of the human immunoglobulin G Fc fragment-binding activity of Mycoplasma salivarium cells by trypsin treatment is ascribed to the binding of trypsin to the Fc fragment.

Human immunoglobulin G Fc fragment-binding activity of Mycoplasma salivarium cells was remarkably enhanced by trypsin treatment of the cells. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis profile of proteins of the cells treated with trypsin was the same as that of the cells treated with pronase, although pronase treatment had been shown to reduce the activity in our previous study (FEMS Microbiol. Lett. 123, 305-310, 1994). This contradiction was clarified by the finding that trypsin bound the Fc fragment more strongly than the cells, and a small amount of trypsin remained in the cells treated with trypsin and washed well. On the basis of these results, it was concluded that the enhancement of cell activity by trypsin treatment was ascribed to binding of the Fc fragment to trypsin remaining in the trypsin-treated cells.

Immunoglobulin Fc Fragments↗

PubMed1992

[The Fc portion of antibodies].

The binding of an antibody to antigen is only the first step of the antigen-antibody reaction. The Fab portions of the antibody determine its specificity and enable the binding of antigen, but the Fc portions is responsible for its biological activity. This biological activity depends on interactions between the Fc portion and specific receptors, Fc Receptor (FcR). FcR are expressed at the surface of many different cell types. Their aggregation by complexed antibodies triggers the activation of cells, which exert their biological activities on antigen-bearing structures. Fc-FcR interactions couple humoral and cellular immunity.

Immunoglobulin Fc Fragments↗