The membrane domain of the human erythrocyte anion transport protein. Epitope mapping of a monoclonal antibody defines the location of a cytoplasmic loop near the C-terminus of the protein
| Autor: | S D Wainwright, W. J. Mawby, Michael J. A. Tanner |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Vesicle-associated membrane protein 8
Immunoblotting Molecular Sequence Data Enzyme-Linked Immunosorbent Assay Biochemistry Epitope Epitopes Residue (chemistry) Anion Exchange Protein 1 Erythrocyte Humans Amino Acid Sequence Molecular Biology Band 3 chemistry.chemical_classification biology C-terminus Antibodies Monoclonal Cell Biology Transport protein Amino acid Epitope mapping chemistry biology.protein Peptides Research Article |
| Zdroj: | Biochemical Journal. 272:265-268 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj2720265 |
| Popis: | We have used synthetic peptides to study the location of the amino acid sequences in the human erythrocyte anion transport protein (band 3) which are recognized by four murine monoclonal antibodies, BRIC 130, 132, 154 and 155. These antibodies are known to react with epitopes in the protein which are on the cytoplasmic side of the membrane. The results suggest that the amino acid residues important for the reaction of BRIC 130 and BRIC 154/155 are located within amino acids 899-908 and 895-901 respectively in the cytoplasmic tail of the protein. The BRIC 132 epitope is located within amino acid residues 813-824. This is part of a surface loop in the protein which probably extends from residue 814 to residue 832 and is located on the cytoplasmic side of the membrane. These results provide direct evidence for the topographical location of a sequence in a poorly understood region of the protein. |
| Databáze: | OpenAIRE |
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