Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 1 of 1
Full-Text Articles in Physical Chemistry
Oxygen Binding Thermodynamics Of Human Hemoglobin In The Red Blood Cell, Kyle K. Hill
Oxygen Binding Thermodynamics Of Human Hemoglobin In The Red Blood Cell, Kyle K. Hill
Department of Chemistry: Dissertations, Theses, and Student Research
We report for the first time the binding constants and Hill numbers for oxygen in the red blood cell under physiological conditions. When compared to our results for hemoglobin in solution, our results show conclusively that hemoglobin binds oxygen more tightly and with lower co-operativity when packed in the red blood cell. At 18°C, these differences are striking: the respective half-saturation values are 15.57 µM (in red blood cells) and 18.83 µM (in solution), with corresponding Hill numbers of 2.475 (in red blood cells) and 2.949 (in solution). The optical complications that arise from high turbidity of red blood cell …