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人类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确定了该蛋白C端附近一个胞质环的位置。

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.

作者信息

Wainwright S D, Mawby W J, Tanner M J

机构信息

Department of Biochemistry, School of Medical Sciences, University of Bristol, U.K.

出版信息

Biochem J. 1990 Nov 15;272(1):265-8. doi: 10.1042/bj2720265.

Abstract

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.

摘要

我们已使用合成肽来研究人红细胞阴离子转运蛋白(带3)中氨基酸序列的位置,这四种鼠单克隆抗体BRIC 130、132、154和155可识别这些序列。已知这些抗体与膜细胞质侧蛋白质中的表位发生反应。结果表明,对BRIC 130和BRIC 154/155反应重要的氨基酸残基分别位于蛋白质细胞质尾部的899 - 908位氨基酸和895 - 901位氨基酸内。BRIC 132表位位于813 - 824位氨基酸残基内。这是蛋白质表面环的一部分,该表面环可能从814位残基延伸至832位残基,且位于膜的细胞质侧。这些结果为该蛋白质一个了解较少区域中序列的拓扑位置提供了直接证据。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3284/1149689/d1716df85ac3/biochemj00171-0256-a.jpg

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