Premium
Inhibition of anion transport across the red cell membrane by dinitrophenylation of a specific lysine residue at the H 2 DIDS binding site of the band 3 protein
Author(s) -
Rudloff V.,
Lepke S.,
Passow H.
Publication year - 1983
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(83)81152-1
Subject(s) - band 3 , dids , chemistry , residue (chemistry) , lysine , stereochemistry , membrane , binding site , dtnb , biochemistry , membrane protein , amino acid , enzyme , glutathione
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 (H 2 DIDS). 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 H 2 DIDS.