PMID: 8960780Nov 1, 1996Paper

Chemical labelling of arginyl-residues involved in anion transport mediated by human band 3 protein and some aspects of its location in the peptide chain

Cellular and Molecular Biology
L ZakiM Merckel

Abstract

The anion exchange system of human red blood cells can be completely inhibited by a large number of arginine-specific reagents. Kinetic studies have shown that these reagents act on the substrate binding site. Complete inhibition of the transport system with 14C phenylglyoxal is accompanied by modification of 2 to 3 arginine residues on the transmembrane segment of band 3. The inhibition and the binding of 14C phenylglyoxal to band 3 is reduced significantly in presence of chloride ions. The interactions between the reversible competitive inhibitor, 4-hydroxy-3-nitrophenylglyoxal (HNPG) and other irreversible anion transport inhibitors with well localized binding sites have been studied. A positive cooperativity between HNPG binding and the inhibition caused by eosin-5-maleimide (EMA), has been measured. Nearly no interactions have been found between HNPG binding site and the histidine residue(s) which react with diethylpyrocarbonate (DEPC). Sulphate self-exchange is irreversibly inhibited by two carboxyl-group reagents, 1-ethyl-3-(3-dimethyl-aminopropyl)carbodiimde (EDC) and N'-(3-dimethylaminopropyl)-N-ethylcarbodiimid methoiodide (EAC), studies on their interaction with the HNPG binding site gave results showing that the rea...Continue Reading

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