Please use this identifier to cite or link to this item:
https://hdl.handle.net/10316/10512
DC Field | Value | Language |
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dc.contributor.author | Rong, Qinfen | - |
dc.contributor.author | Espanol, Maryceline | - |
dc.contributor.author | Freitas, Duarte Mota de | - |
dc.contributor.author | Geraldes, Carlos F. G. C. | - |
dc.date.accessioned | 2009-07-07T08:21:42Z | - |
dc.date.available | 2009-07-07T08:21:42Z | - |
dc.date.issued | 1993-12 | - |
dc.identifier.citation | Biochemistry. 32:49 (1993) 13490-13498 | en_US |
dc.identifier.issn | 0006-2960 | - |
dc.identifier.uri | https://hdl.handle.net/10316/10512 | - |
dc.description.abstract | We used 7Li NMR spin-lattice (TI) and spin-spin (Tz) relaxation time measurements to investigate the binding of Li+ in human red blood cell (RBC) suspensions. In RBCs containing 1.4 mM Li+, the intracellular 7Li NMR T2 relaxation value (0.30 f 0.03 s) was much smaller than the corresponding TI value (6.0 f 0.1 s), yielding a ratio of TI to T2 of 20. For 1.5 mM LiCl solutions whose viscosities were adjusted to 5 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 Tl/ T2 ratios observed in Li+-loaded RBCs. We conclude that the RBC membrane is the major Li+ binding site in Li+-loaded RBCs (KI=, 215 f 36 M-l) and that the binding of Li+ to COHb, BPG, spectrin-actin, or ATP is weak. Partially relaxed 7Li 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 TI 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. | en_US |
dc.language.iso | eng | en_US |
dc.publisher | American Chemical Society | en_US |
dc.rights | openAccess | eng |
dc.title | Lithium-7 NMR relaxation study of lithium binding in human erythrocytes | en_US |
dc.type | article | en_US |
dc.identifier.doi | 10.1021/bi00212a014 | - |
uc.controloAutoridade | Sim | - |
item.fulltext | Com Texto completo | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.languageiso639-1 | en | - |
item.openairetype | article | - |
item.cerifentitytype | Publications | - |
item.grantfulltext | open | - |
crisitem.author.researchunit | CQC - Coimbra Chemistry Centre | - |
crisitem.author.parentresearchunit | Faculty of Sciences and Technology | - |
crisitem.author.orcid | 0000-0002-0837-8329 | - |
Appears in Collections: | FCTUC Ciências da Vida - Artigos em Revistas Internacionais |
Files in This Item:
File | Description | Size | Format | |
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Lithium-7 NMR relaxation study of lithium.pdf | 1.18 MB | Adobe PDF | View/Open |
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