2026 Summer Undergraduate Research Program (SURP) Symposium
Location
Schindler Education Center, University of Northern Iowa
Presentation Type
Open Access Poster Presentation
Document Type
poster
Abstract
Hemoglobin oxygen affinity is influenced by intracellular pH through the Bohr effect, making pH an important regulator of oxygen delivery throughout the body. Before oxygen-binding affinity can be quantified, the optical properties of hemoglobin under different pH conditions must first be characterized. In this study, free hemoglobin was analyzed at five physiologically relevant pH values (6.72, 7.00, 7.33, 7.63, and 7.92), representing conditions ranging from acidosis to alkalosis. Human red blood cells were lysed in hypotonic phosphate solutions, and absorbance spectra were collected using a scanning spectrophotometer. The resulting spectra establish baseline optical characteristics of hemoglobin across physiologically relevant pH values and provide the foundation for future studies measuring oxygen-binding affinity in intact red blood cells maintained under controlled intracellular conditions.
Start Date
31-7-2026 11:00 AM
End Date
31-7-2026 1:30 PM
Event Host
Summer Undergraduate Research Program, University of Northern Iowa
Faculty Advisor
Carl L. Thurman
Department
Department of Biology
Copyright
©2026 Anna N. Gregorsok and Carl L. Thurman
File Format
application/pdf
File Size
962 KB
Recommended Citation
Gregorsok, Anna N. and Thurman, Carl L., "Analyzing the Effect of Physical and Chemical Properties on Spectral Absorption of Hemoglobin" (2026). Summer Undergraduate Research Program (SURP) Symposium. 4.
https://scholarworks.uni.edu/surp/2026/all/4
Analyzing the Effect of Physical and Chemical Properties on Spectral Absorption of Hemoglobin
Schindler Education Center, University of Northern Iowa
Hemoglobin oxygen affinity is influenced by intracellular pH through the Bohr effect, making pH an important regulator of oxygen delivery throughout the body. Before oxygen-binding affinity can be quantified, the optical properties of hemoglobin under different pH conditions must first be characterized. In this study, free hemoglobin was analyzed at five physiologically relevant pH values (6.72, 7.00, 7.33, 7.63, and 7.92), representing conditions ranging from acidosis to alkalosis. Human red blood cells were lysed in hypotonic phosphate solutions, and absorbance spectra were collected using a scanning spectrophotometer. The resulting spectra establish baseline optical characteristics of hemoglobin across physiologically relevant pH values and provide the foundation for future studies measuring oxygen-binding affinity in intact red blood cells maintained under controlled intracellular conditions.
