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Anion transport in red blood cells and arginine‐specific reagents
Author(s) -
Zaki Laila
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80325-7
Subject(s) - phenylglyoxal , band 3 , reagent , chemistry , arginine , anion exchanger , chymotrypsin , mole , chromatography , membrane , biochemistry , ion , ion exchange , erythrocyte membrane , enzyme , amino acid , organic chemistry , trypsin
The reaction of phenylglyoxal, a reagent specific for arginine residues, with erythrocyte membrane at pH 7.4 results in complete inhibition of sulfate equilibrium exchange across human red cells. The inactivation was found to be concentration and time depenent. The binding sites of this reagent in the anion transport protein (band 3) under these conditions were determined by using [ 14 C]phenylglyoxal. The rate of incorporation of the radioactivity into band 3 gave a good correlation with the rate of inactivation. Under conditions where the transport is completely inhibited about 6 mol [ 14 C]phenylglyoxal are incorporated into 1 mol band 3. Treating the [ 14 C]phenylglyoxalated ghosts at different degrees of inactivation with extracellular chymotrypsin showed that about two‐thirds of these binding sites are located on the 60 kDa fragment.