Literature DB >> 7099165

The interaction of the Facb fragment of rabbit anti-sheep red cell IgG with guinea pig macrophages, and human monocytes and granulocytes.

D E Barnett-Foster, R H Painter.   

Abstract

Yasmeen et al. (J. Immun. 110, 1706-1709, 1973) have previously reported on the binding requirements of the guinea pig peritoneal macrophage Fc receptor. The C gamma 3 domain fragments of human IgG1, in contrast to the C gamma 2 domain fragment, were able to bind to these macrophages, as demonstrated by both direct and indirect rosette tests. We now report that we have been unable to show binding by the C gamma 2-bearing rabbit Facb fragment to either peritoneal or alveolar macrophages of the guinea pig. This evidence is therefore in agreement with the hypothesis proposed by Yasmeen et al. (1973) that the C gamma 2 homology region does not contribute directly to the binding requirements for this cell type. The same protein, rabbit anti-sheep erythrocyte Facb, when coated on sheep erythrocytes, did not form rosettes with human granulocytes, but did form some rosettes with human monocytes.

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Year:  1982        PMID: 7099165     DOI: 10.1016/0161-5890(82)90337-6

Source DB:  PubMed          Journal:  Mol Immunol        ISSN: 0161-5890            Impact factor:   4.407


  1 in total

1.  Isolation and identification of a biologically active peptide derived from the CH3 domain of human IgG1.

Authors:  E L Morgan; T E Hugli; W O Weigle
Journal:  Proc Natl Acad Sci U S A       Date:  1982-09       Impact factor: 11.205

  1 in total

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