THE AMINO-ACID CONJUGATE FORMED BY THE INTERACTION OF THE ANION TRANSPORT INHIBITOR 4,4'-DIISOTHIOCYANO-2,2'-STILBENEDISULFONIC ACID (DIDS) WITH BAND 3-PROTEIN FROM HUMAN RED-BLOOD-CELL MEMBRANES
THE AMINO-ACID CONJUGATE FORMED BY THE INTERACTION OF THE ANION TRANSPORT INHIBITOR 4,4'-DIISOTHIOCYANO-2,2'-STILBENEDISULFONIC ACID (DIDS) WITH BAND 3-PROTEIN FROM HUMAN RED-BLOOD-CELL MEMBRANES
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DOI：
10.1016/0005-2736(81)90581-2
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发表时间：
1981-01-01
期刊：
影响因子：
--
通讯作者：
ROTHSTEIN, A
中科院分区：
文献类型：
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作者：
RAMJEESINGH, M;GAARN, A;ROTHSTEIN, A
特异性阴离子转运抑制剂4，4''-二异硫氰基-2，2''-二苯乙烯二磺酸(DIDS)及其还原类似物(H2DIDS)当不可逆地结合至红细胞膜的带3蛋白时，通过与特定赖氨酸残基的ε-氨基相互作用形成氨基酸缀合物。该特定残基位于带 3 蛋白的跨膜片段中，并且似乎是转运位点的近邻。
The specific anion transport inhibitor 4,4''-diisothiocyano-2,2''-stilbenedisulfonic acid (DIDS) and its reduced analog (H2DIDS), when irreversibly bound to band 3 protein of the red blood cell membrane, form amino acid conjugates through interaction with the .epsilon.-amino group of a particular lysine residue. The specific residue is located in a transmembrane segment of band 3 protein and appears to be a close neighbor of the transport site.