Anion transport in red blood cells and arginine‐specific reagents

FEBS Letters

Zaki, Laila¹ 

[1] Max-Planck-Institut für Biophysik, 6000 Frankfurt am Main 71, FRG

关键词: Anion transport;    Band 3;    Arginine-specific reagent;    PG;    phenylglyoxal;    H2DIDS;    4;    4-diisothiocyanodihydrostilbene-2;    2-disulfonate;    SITS;    4-acetamido-4-isothiocyanostilbene-2;    2-disulfonic acid;    DNFB;    1-fluoro-2;    4-dinitrobenzene;   

DOI  :  10.1016/0014-5793(84)80325-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 [¹⁴C]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 [¹⁴C]phenylglyoxal are incorporated into 1 mol band 3. Treating the [¹⁴C]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.

【 授权许可】

Unknown