Red blood cell band 3. Lysine 539 and lysine 851 react with the same H2DIDS (4,4‘-diisothiocyanodihydrostilbene-2,2‘-disulfonic acid) molecule.
نویسندگان
چکیده
منابع مشابه
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.
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 reacti...
متن کاملCharacterization of the stilbenedisulphonate binding site on band 3 Memphis variant II (Pro-854-->Leu).
Band 3 Memphis variant II is a mutant anion-exchange protein associated with the Diego a+ blood group antigen. There are two mutations in this transporter: Lys-56-->Glu within the cytoplasmic domain, and Pro-854-->Leu within the membrane-bound domain. The Pro-854 mutation, which is thought to give rise to the antigenicity, is located within the C-terminal subdomain of the membrane-bound domain....
متن کاملO-Methylisourea Can React with the α-Amino Group of Lysine: Implications for the Analysis of Reactive Lysine
The specificity of O-methylisourea (OMIU) to bind to the ε-amino group of Lys, an important supposition for the OMIU-reactive Lys analysis of foods, feeds, ingredients, and digesta, was investigated. Crystalline l-Lys incubated under standard conditions with OMIU resulted in low homoarginine recoveries. The reaction of OMIU with the α-amino group of Lys was confirmed by MS analysis, with double...
متن کاملA Basis of the Stomatocytoses of Erythrocytes by 1-Chloro-2, 4- Dinitrobenzene and Other Electrophilic Reagents
On bases of previous observations on the band 3 anion exchange inhibition by the electrophilic reagent 1-fluoro-2,4-dinitrobenzene in resealed ghosts and a previously proposed band 3-based mechanism of control of the erythrocyte shape, it is suggested that stomatocytoses by 1-chloro-2,4-dinitrobenzene and other electrophilic reagents are due to an inhibition of the band 3 anion exchange by a co...
متن کاملHuman erythrocyte protein 4.2 deficiency associated with hemolytic anemia and a homozygous 40glutamic acid-->lysine substitution in the cytoplasmic domain of band 3 (band 3Montefiore).
Red blood cell (RBC) protein 4.2 deficiency is often associated with a moderate nonimmune hemolytic anemia, splenomegaly, and osmotically fragile RBCs resembling, but not identical to, hereditary spherocytosis (HS). In the Japanese type of protein 4.2 deficiency (protein 4.2Nippon), the anemia is associated with a point mutation in the protein 4.2 cDNA. In this report, we describe a patient wit...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1994
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)42114-4