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Phosphorus-31 relaxation times of 2,3-diphosphoglycerate in intact human erythrocytes
Authors:Harry J Lubansky  Akira Omachi  CTyler Burt
Institution:1. Department of Physiology and Biophysics, University of Illinois at the Medical Center, 901 South Wolcott Street Chicago, Illinois 60612 USA;2. Department of Biological Chemistry, University of Illinois at the Medical Center, 901 South Wolcott Street Chicago, Illinois 60612 USA
Abstract:The reciprocals of the spin-lattice relaxation times (T1s) of the 2-P and 3-P nuclei of 2,3-diphosphoglycerate (DPG) increased linearly as percent DPG bound was raised in model hemoglobin solutions. The 2-P T1 was slightly greater in intact erythrocytes than in model solutions under similar experimental conditions. The change in the 3-P T1 with cellular deoxygenation was anomalous indicating that this nucleus should not be used to estimate DPG binding inside intact erythrocytes.
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