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Unformatted text preview: Lecture 30: Respiratory Physiology III Reading: ch 13, section: pgs 484-487. (pgs 492-495, if using 5 rd edition) Oxygen storage- hemoglobin serves as a reservoir for O 2 without affecting the partial pressure gradient that is necessary for gas exchange (Figure 13-28) . Hemoglobin- this is a soluble protein present in the cytoplasm of erythrocytes (red blood cells) that can reversibly bind 4 molecules of O 2 (Figure 11-3) to a specialized iron- containing component referred to as a heme group. Hemoglobin has 4 heme groups (each with an iron atom), each of which can reversibly combine with an O 2 molecule. Hb + O 2 ↔ HbO 2 reduced hemoglobin oxyhemoglobin ( DEOXYGENATED ) ( RED IN COLOR ) hemoglobin saturation- hemoglobin is considered fully saturated when all of the Hb present in the blood is carrying its maximum load of O 2 . The extent of Hb saturation in the blood can vary from 0% to 100%. The most important factor determining the % Hb saturation is the P O2 of the blood, which is related to the concentration of O 2 dissolved in the blood. The % Hb saturation is proportional to the P O2 of the blood and this relationship follows a non-linear S-shaped function known as the oxygen-hemoglobin dissociation curve (Figure 13-27) . Several physiological factors can influence the properties of the dissociation curve (Figure 13-29) ....
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This note was uploaded on 05/02/2008 for the course NPB 101 taught by Professor Fuller,charles/goldberg,jack during the Winter '08 term at UC Davis.
- Winter '08