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Titolo:
LI-7 NMR RELAXATION STUDY OF LI+ BINDING IN HUMAN ERYTHROCYTES
Autore:
RONG QF; ESPANOL M; DEFREITAS DM; GERALDES CFGC;
Indirizzi:
LOYOLA UNIV,DEPT CHEM,6525 N SHERIDAN RD CHICAGO IL 60626 LOYOLA UNIV,DEPT CHEM,6525 N SHERIDAN RD CHICAGO IL 60626 UNIV COIMBRA,DEPT BIOCHEM P-3000 COIMBRA PORTUGAL UNIV COIMBRA,CTR NEUROSCI P-3000 COIMBRA PORTUGAL
Titolo Testata:
Biochemistry
fascicolo: 49, volume: 32, anno: 1993,
pagine: 13490 - 13498
SICI:
0006-2960(1993)32:49<13490:LNRSOL>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; RED-BLOOD-CELLS; MANIC-DEPRESSIVE PATIENTS; LITHIUM TRANSPORT; ESSENTIAL-HYPERTENSION; SPIN RELAXATION; MEMBRANE; ION; PHOSPHATIDYLSERINE; NA+;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
69
Recensione:
Indirizzi per estratti:
Citazione:
Q.F. Rong et al., "LI-7 NMR RELAXATION STUDY OF LI+ BINDING IN HUMAN ERYTHROCYTES", Biochemistry, 32(49), 1993, pp. 13490-13498

Abstract

We used Li-7 NMR spin-lattice (T1) and spin-spin (T2) relaxation timemeasurements to investigate the binding of Li+ in human red blood cell (RBC) suspensions. In RBCs containing 1.4 mM Li+, the intracellular Li-7 NMR T2 relaxation value (0.30 +/- 0.03 s) was much smaller than the corresponding T1 value (6.0 +/- 0.1 s), yielding a ratio of T1 to T2 of 20. For 1. 5 mM LiCl solutions whose viscosities were adjusted to5 cP with glycerol, the values of the T1/T2 ratios were as follows: 49 for unsealed RBC membrane (2.0 mg of protein/mL); 4.4 for spectrin (1.9 mg/mL); 1.5 for 5.4 mM 2,3-bisphosphoglycerate (BPG); 2.2 for 2.7 mM carbonmonoxyhemoglobin (COHb); 1.6 for 2.0 mM ATP; and 1.2 for a 50/50% (v/v) glycerol-water mixture. Intracellular viscosity and the electric field gradients experienced by Li+ when traversing the spectrin-actin network therefore are not responsible for the large values of the T1/T2 ratios observed in Li+-loaded RBCs. We conclude that the RBC membrane is the major Li+ binding site in Li+-loaded RBCs (K(b) = 215 +/- 36 M-1) and that the binding of Li+ to COHb, BPG, spectrin-actin, or ATP is weak. Partially relaxed Li-7 NMR spectra of Li+-containing RBC membrane suspensions indicated the presence of two relaxation components, one broad and one narrow. At the same extravesicular Li+ and protein concentrations, the T1 values for right-side-out RBC vesicle suspensions were at least 2-fold larger than those for inside-out RBC vesicle suspensions; the inner layer of the RBC membrane, which has a larger percentage of anionic phospholipids than the outer layer, contributes mostly to Li+ binding.

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Documento generato il 04/12/20 alle ore 19:28:19