Date of Award

8-31-2018

Document Type

Campus Access Thesis

Degree Name

Master of Science (MS)

Department

Physics, Applied

First Advisor

Chandra Yelleswarapu

Second Advisor

Stephen Arnason

Third Advisor

Jonathan Celli

Abstract

Oxygen is often called the molecule of life. It is very important to every cell in our body. Oxygen is carried from lungs to the rest of the body by hemoglobin in the blood. As each hemoglobin molecule can carry a maximum of four oxygen molecules, oxygen saturation (SO2) is the measure of percentage of oxygen content in blood. Desired SO2 levels in a healthy human being are between 95 to 100 percent. A reading lower than 90 percent is considered a clinical emergency. Therefore measuring and monitoring of SO2 levels in blood is very important in medicine. Two main derivatives of hemoglobin are oxyhemoglobin (HbO2) and deoxyhemoglobin (Hb). Their distinct spectral profiles in the near-infrared region are used to measure blood oxygen saturation, such as in pulse oximetry. Further the distinction has been used in biomedical imaging as endogenous contrast. The purpose of this work is to test whether Lyophilized powder (human hemoglobin protein) can be used, instead of real blood, to measure the SO2 levels in a research environment. HbO2 and Hb samples were prepared by dissolving protein powder in water and PBS (phosphate buffer solution) and their SO2 levels were measured using UV-Vis spectrometer. Results show that the spectral profiles of the prepared samples resemble methemoglobin and carboxyhemoglobin instead of oxyhemoglobin and deoxyhemoglobin. Reasons for not being able to prepare HbO2 and Hb samples and potential future directions are discussed.

Comments

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