Effects of chemical modification of cysteines 201 and 317 of band 3 on hemolytic properties of human erythrocytes under hydrostatic pressure.
In the membrane stability of human erythrocytes, the role of two cysteine residues (Cys-201 and Cys-317) in the cytoplasmic domain of band 3 is not clear. So we tried to resolve this problem by examining hemolytic properties under high pressure. From SH contents and spin labeling, it was found that Cys-201 and Cys-317 of band 3 were modified with N-ethylmaleimide (NEM). The hemolysis of intact erythrocytes at 200 MPa was suppressed by the binding of 4, 4'-diisothiocyanostilbene-2,2'-disulfonate (DIDS), anion transport inhibitor, to band 3. Similarly, the suppressive effect of DIDS was observed in the erythrocyte that Cys-201 and Cys-317 were modified with NEM. These results suggest that the cysteine residues in the cytoplasmic domain of band 3 are not essential for the DIDS-induced membrane stabilization.
Yamaguchi
T
T
Department of Chemistry, Faculty of Science, Fukuoka University, Jonan-ku, Fukuoka, 814-0180, Japan. takeo@ssat.fukuoka-u.ac.jp
Nakano
T
T
Matsumoto
M
M
Terada
S
S
D017878:4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid / Q000494:pharmacology; D001457:Anion Exchange Protein 1, Erythrocyte / Q000737:chemistry*; D000838:Anions; D003545:Cysteine / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000737:chemistry / Q000187:drug effects*; D005033:Ethylmaleimide / Q000737:chemistry; D006461:Hemolysis / Q000187:drug effects*; D006801:Humans; D017136:Ion Transport / Q000187:drug effects; D011312:Pressure; D013113:Spin Labels
D001457:Anion Exchange Protein 1, Erythrocyte; D000838:Anions; D013113:Spin Labels; D003545:Cysteine; D005033:Ethylmaleimide; D017878:4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid