Biosynthesis of the erythrocyte anion transport protein.
نویسندگان
چکیده
منابع مشابه
Biosynthesis of the erythrocyte anion transport protein.
The biosynthesis of the erythrocyte anion transport protein (Band III) was studied in erythroid precursor cells obtained from the spleens of anemic mice. Newly synthesized Band III was inserted during or immediately after translation into rough endoplasmic reticulum membranes. The asymmetric orientation of Band III in these membranes resembled that of mature Band III in erythrocyte membranes, w...
متن کاملSelective phenylglyoxalation of functionally essential arginyl residues in the erythrocyte anion transport protein
The red cell anion transport protein, band 3, can be selectively modified with phenylglyoxal, which modifies arginyl residues (arg) in proteins, usually with a phenylglyoxal: arg stoichiometry of 2:1. Indiscriminate modification of all arg in red cell membrane proteins occurred rapidly when both extra- and intracellular pH were above 10. Selective modification of extracellularly exposed arg was...
متن کاملCharacterization of matrix-bound Band 3, the anion transport protein from human erythrocyte membranes.
Band 3 (Mr = 95,000), the anion transport protein of human erythrocyte membranes exists primarily as a dimer in solutions of nonionic detergents such as octaethylene glycol mono-n-dodecyl ether (C12E8). The role of the oligomeric structure of Band 3 in the binding of [14C]4-benzamido-4'-aminostilbene-2,2'-disulfonate (BADS), an inhibitor of anion transport (Ki = 1-2 microM), was studied by char...
متن کاملFunctions of extracellular lysine residues in the human erythrocyte anion transport protein
The extracellular lysine residues in the human erythrocyte anion transport protein (band 3) have been investigated using chemical modification with the impermeant homobifunctional active ester bis(sulfosuccinimidyl)-suberate (BSSS). This agent forms covalent intra- and intermolecular cross-links in human band 3 in intact cells (Staros and Kakkad. 1983. J. Membr. Biol. 74:247). We have found tha...
متن کاملThe human erythrocyte anion transport protein, band 3. Characterization of exofacial alkaline titratable groups involved in anion binding/translocation
Chloride self-exchange across the human erythrocyte membrane at alkaline extracellular pH (pHO) and constant neutral intracellular pH (pH(i)) can be described by an exofacial deprotonatable reciprocating anion binding site model. The conversion of the transport system from the neutral to the alkaline state is related to deprotonation of a positively charged ionic strength- and substrate-sensiti...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1981
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)68596-0