caa a22 4500 477132456 CHVBK 20180405111707.0 cr unu---uuuuu 170330e19971201xx s 000 0 eng 10.1023/A:1018324416694 doi (NATIONALLICENCE)springer-10.1023/A:1018324416694 Binding of vanadate to human erythrocyte ghosts and subsequent events [Elektronische Daten] [Boyan Zhang, Li Ruan, Baowei Chen, Jinfen Lu, Kui Wang] Spectroscopic techniques were used to investigate the interaction between vanadate and human erythrocyte ghosts. Direct evidence from 51V nuclear magnetic resonance (NMR) studies suggested that the monomeric and polymeric vanadate species may bind to the anion binding sites of band 3 protein of the erythrocyte membrane. The results of 51V NMR studies and the quenching effect of vanadate on the intrinsic fluorescence of the membrane proteins indicated that in the low concentration range of vanadate (<0.6 mm), monomeric vanadate binds mostly to the anion sites of band 3 protein with the dissociation constant close to 0.23 mm. The experiments of sulfhydryl content titration by the method of Ellman and residue sulfhydryl-labeled fluorescence spectroscopies clearly displayed that vanadate reacts directly with sulfhydryl groups. The appearance of the anisotropic election spin resonance (ESR) signal of vanadyl suggests that a small (c. 3%) amount of vanadate was reduced by sulfhydryl groups of membrane proteins. The fluidity and order of intact ghost membrane were reduced by the reaction with vanadate, as shown by the ESR studies employing the protein- and lipid-specific spin labels. It was concluded that although vanadates mainly bind to band 3 protein, a minor part of vanadate may oxidize the residue sulfhydryl groups of membrane proteins, and thus decrease the fluidity of erythrocyte membrane. Chapman and Hall, 1997 band 3 protein nationallicence erythrocyte membrane nationallicence membrane fluidity nationallicence sulfhydryl groups nationallicence vanadate nationallicence Zhang Boyan Inorganic Chemistry Department, School of Pharmaceutical Sciences, Beijing Medical University, Beijing, China aut Ruan Li Inorganic Chemistry Department, School of Pharmaceutical Sciences, Beijing Medical University, Beijing, China aut Chen Baowei Inorganic Chemistry Department, School of Pharmaceutical Sciences, Beijing Medical University, Beijing, China aut Lu Jinfen Inorganic Chemistry Department, School of Pharmaceutical Sciences, Beijing Medical University, Beijing, China aut Wang Kui Inorganic Chemistry Department, School of Pharmaceutical Sciences, Beijing Medical University, Beijing, China aut Biometals Kluwer Academic Publishers 10/4(1997-12-01), 291-298 0966-0844 10:4<291 1997 10 10534 https://doi.org/10.1023/A:1018324416694 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1018324416694 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Zhang Boyan Inorganic Chemistry Department, School of Pharmaceutical Sciences, Beijing Medical University, Beijing, China aut NATIONALLICENCE 700 1- Ruan Li Inorganic Chemistry Department, School of Pharmaceutical Sciences, Beijing Medical University, Beijing, China aut NATIONALLICENCE 700 1- Chen Baowei Inorganic Chemistry Department, School of Pharmaceutical Sciences, Beijing Medical University, Beijing, China aut NATIONALLICENCE 700 1- Lu Jinfen Inorganic Chemistry Department, School of Pharmaceutical Sciences, Beijing Medical University, Beijing, China aut NATIONALLICENCE 700 1- Wang Kui Inorganic Chemistry Department, School of Pharmaceutical Sciences, Beijing Medical University, Beijing, China aut NATIONALLICENCE 773 0- Biometals Kluwer Academic Publishers 10/4(1997-12-01), 291-298 0966-0844 10:4<291 1997 10 10534 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer