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Human transcobalamin II receptor binds to Staphylococcus aureus protein A: Implications as to its structure and function
- Source :
-
Archives of Biochemistry & Biophysics . Mar2003, Vol. 411 Issue 2, p204. 11p. - Publication Year :
- 2003
-
Abstract
- Purified human placental transcobalamin II receptor (TC II-R) dimer of molecular mass 124 kDa bound to Sepharose-linked bacterial immunoglobulin (IgG) binding proteins protein A, protein G, and protein A/G. TC II-R dimer was detected directly, by blotting human placental and rabbit and rat kidney membrane proteins with 125I-protein A, or indirectly, using antiserum to TC II-R or IgG–Fc region and 125I-protein. TC II-R antiserum, but not protein A, protein G, protein A/G, or antiserum to the IgG–Fc region, when added to culture medium of human intestinal epithelial Caco-2 cells or umbilical vein endothelial cells, inhibited ligand binding. However, protein A, protein G, protein A/G, or antiserum to the Fc region inhibited the internalization of the ligand TC II-[57Co]cyanocobalamin. Taken together, these studies strongly suggest TC II-R is an IgG-like molecule that contains an Fc-like region which is important in ligand internalization but not binding. [Copyright &y& Elsevier]
- Subjects :
- *MEMBRANE proteins
*PROTEIN binding
Subjects
Details
- Language :
- English
- ISSN :
- 00039861
- Volume :
- 411
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Archives of Biochemistry & Biophysics
- Publication Type :
- Academic Journal
- Accession number :
- 9193765
- Full Text :
- https://doi.org/10.1016/S0003-9861(03)00005-5