Inhibition of anion transport across the red cell membrane by dinitrophenylation of a specific lysine residue at the H2DIDS binding site of the band 3 protein

FEBS Letters

Rudloff, V.¹  Passow, H.¹  Lepke, S.¹ 

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

关键词: Band 3 protein;    Anion transport;    1-Fluoro 2;    4-dinitrobenzene;    H2DIDS;    Erythrocyte;    N2ph-F;    1-fluoro-2;    4-dinitrobenzene;    H2DIDS;    4;    4'-diisothiocyano dihydrostilbene-2;    2'-disulfonate;    DNDS;    4;    4'-dinitro stilbene-2;    2'-disulfonate;    SITS;    4-isothiocyano 4'-acetamido stilbene-2;    2'-disulfonate;    PCMBS;    p-chloro mercuribenzene sulfonate;    EDTA;    ethylene diamine tetra acetic acid;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/0014-5793(83)81152-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The inhibition of anion transport by dinitrophenylation of the red cell membrane is brought about by the modification of a single lysine residue located on the 17-kDa segment of the band 3 protein. This residue is identical with Lys a, which is also capable of reacting with one of the two isothiocyanate groups of 4,4'-diisothiocyano dihydro-stilbene-2,2'-disulfonate (H₂DIDS). The rate of reaction between Lys a and 1-fluoro-2,4-dinitrobenzene is reduced when a second lysine residue on the 35-kDa segment of the band 3 protein becomes dinitrophenylated. This latter residue is not identical with Lys b which is known to be present on the 35-kDa segment and involved in the cross-linking of this segment with the 17-kDa segment by H₂DIDS.

【 授权许可】

Unknown