首页> 美国卫生研究院文献>Biochemical Journal >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.
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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.

机译:人红细胞阴离子转运蛋白的膜结构域。单克隆抗体的表位作图定义了蛋白质C端附近的细胞质环的位置。

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摘要

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.
机译:我们已使用合成肽研究了人类红细胞阴离子运输蛋白(条带3)中氨基酸序列的位置,该序列被四种鼠类单克隆抗体BRIC 130、132、154和155识别。已知这些抗体会与蛋白质的抗原决定簇位于膜的细胞质侧。结果表明,对于BRIC 130和BRIC 154/155的反应重要的氨基酸残基分别位于蛋白质的细胞质尾部的氨基酸899-908和895-901内。 BRIC 132表位位于氨基酸残基813-824内。这是蛋白质中表面环的一部分,其可能从残基814延伸至残基832,并位于膜的细胞质侧。这些结果为该序列在蛋白质的鲜为人知的区域中的拓扑位置提供了直接的证据。

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