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.
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.
Department of Biochemistry, School of Medical Sciences, University of Bristol, U.K.
S D
SD
Wainwright
W J
WJ
Mawby
M J
MJ
Tanner
D000595:Amino Acid Sequence; D001457:Anion Exchange Protein 1, Erythrocyte / Q000737:chemistry* / Q000276:immunology; D000911:Antibodies, Monoclonal; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000737:chemistry*; D006801:Humans; D015151:Immunoblotting; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis
D001457:Anion Exchange Protein 1, Erythrocyte; D000911:Antibodies, Monoclonal; D000939:Epitopes; D010455:Peptides