Oxygen Dissociation Curve PDF
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Tamethia Perkins
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This document explains oxygen transport, focusing on the oxygen dissociation curve and its clinical significance. It discusses how oxygen is carried, chemical reactions involved, and factors affecting this process. It covers topics such as dissolved oxygen, hemoglobin binding, and different forms of tissue hypoxia.
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OXYGEN TRANSPORT Tamethia Perkins MS, RRT-NPS, RRT-ACCS RT 3005/6005 OXYGEN TRANSPORT ◼ How O2 is transported to the tissues ◼ O2 dissociation curve and its clinical significance ◼ O2 transport studies to identify patient’s cardiac and ventilatory status ◼ Major form...
OXYGEN TRANSPORT Tamethia Perkins MS, RRT-NPS, RRT-ACCS RT 3005/6005 OXYGEN TRANSPORT ◼ How O2 is transported to the tissues ◼ O2 dissociation curve and its clinical significance ◼ O2 transport studies to identify patient’s cardiac and ventilatory status ◼ Major forms of tissue hypoxia OXYGEN TRANSPORT ◼ Transported in two forms: ◼ Dissolved in the plasma ◼ Bound to Hgb DISSOLVED OXYGEN ◼ Once O2 enters the plasma, it moves freely throughout the plasma in its normal gaseous state. ◼ This is the portion of O2 measured clinically (PO2). ◼ At normal T, about 0.003mL of O2 will dissolve in 100 mL of blood for every 1 mmHg of PO2. ◼ 0.003 = solubility coefficient. ◼ Normal PO2 = 100 mmHg = 0.3 mL is dissolved in every 100 mL of blood. O2 BOUND TO HEMOGLOBIN HEMOGLOBIN ◼ Each RBC has ~280 million Hb molecules. ◼ Normal HbA consists of: ◼ 4 heme groups. ◼ Iron-containing non-protein portion ◼ 4 amino acid chains (polypeptide) that constitute a globin (protein). HEMOGLOBIN ◼ Iron can combine with one O2 molecule in a reversible reaction to form oxyHb. ◼ Hb (reduced Hb or deoxyHb) + O 2 = HbO2 ◼ When 4 molecules are bound to one Hb molecule: Hb is 100% saturated. ◼ Globin portion: 2 alpha and beta chains. ◼ Changes in the aa sequence alters normal structure of the Hb. ◼ Sickle cell Hb (HbS) = different B chain = changes morphology of the RBC. HEMOGLOBIN ◼ Normal Hb: 14-16 g/dL to 12-15 g/dL. ◼ Normal infant Hb: 14-20 g/dL. OXYGEN BOUND TO Hb ◼ Each gram of Hb is capable of carrying 1.34 mL of O 2. ◼ If Hb is 15 g% and 100% saturated = 20 vol%. (HbO 2 = 1.34 mLO2 x 15g%) =20 vol %. ◼ Normal Hb sat is 97% ◼ Thebesian veins, bronchial veins, underventilated alveoli. TOTAL O2 CONTENT ◼ HbO2 + dissolved O2 ◼ CaO2 = (Hb x 1.34 x SaO2) + (PaO2 x 0.003) = normal 20 vol% O2 transport (DO2) ◼ Good indication of cardiopulmonary Function ◼ CO x (CaO2 x 10) ◼ Normal 900 – 1150 ml O2/min O2 DISSOCIATION CURVE Oxygen Dissociation Curve ◼ Illustrates percentage of Hb that is chemically bound to O2 at each PO2. ◼ S-shaped with a steep slope between 10 and 60 mmHg, and a flat portion between 70 and 100 mmHg. ◼ Steep: rapid combination of Hb and O2. ◼ Flat: further increase in PO2 induces a slight change in Hb saturation. Clinical Importance of the Flat Portion of the Curve ◼ PO2 can fall from 100 mmHg to 60 mmHg and Hb saturation will be ~90%. ◼ This plateau becomes a safety zone for uploading of O2 in the lungs. ◼ As Hb moves through the alveolo-capillary system to pick up O2, a significant PO2 continues to exist between alveolar gas and blood even after most of the O2 is transferred= enhances diffusion. Clinical Importance of the Flat Portion of the Curve ◼ Flat portion also means that increasing PO2 beyond 100 mmHg adds very little additional O2 to the blood. Clinical Importance of the Steep Portion of the Curve ◼ PO2 reductions below 60 mmHg cause a rapid decrease in the amount of O2 bound to Hb = decrease O2 delivery to the tissues. P50 ◼ Partial P of O2 at which the Hb is 50% saturated. ◼ NORMAL: 27 mmHg ◼ When P50 increases: ◼ Shift to the R: low affinity of Hb for O 2. ◼ When P50 decreases: ◼ Shift to the L: high affinity of Hb for O 2. FACTORS THAT SHIFT THE CURVE pH ◼ High [H+]= low pH = shift to R ◼ Improves unloading O 2 to the tissues. ◼ Low [H+] = high pH = shift to L ◼ Improves uploading of O2 in the lungs Temperature ◼ High T = shift to R ◼ Low T = shift to L ◼ Cyanosis while swimming in very cold water. ◼ PaO2 is normal but Hb is not releasing the O2. FACTORS THAT SHIFT THE CURVE CO2 ◼ High CO2 = low pH = shift to R ◼ Low CO2 = high pH = shift to L ◼ Improves uploading of O2 in the lungs. 2,3-Diphosphoglycerate (2,3-DPG) ◼ RBCs contain large amounts of 2,3-DPG. ◼ Formed during anerobic glycolisis. ◼ High 2,3-DPG = shift to R. ◼ Hypoxia, anemia, low pH = high 2,3-DPG. ◼ Stored blood = low 2,3-DPG = low PO2 tissues. FACTORS THAT SHIFT THE CURVE Fetal Hb (Hb F) ◼ HbF has greater affinity (L) for O2 than HbA. ◼ During fetal development, higher affinity enhances transfer of O2 from maternal blood to fetal blood. ◼ HbF progressively dissappears >1y. Carbon Monoxide Hb (COHb) ◼ CO has 210 times more affinity for Hb than O2. ◼ Small amounts of CO can tie Hb. ◼ Prevents O2 from binding to Hb. ◼ Shifts the curve to the L = limited unloading to the tissues. CLINICAL APPLICATION ◼ When PaO2 is normal (80-100 mmHg), a shift to the R or L does not significantly affect Hb’s ability to transport O2 to the tissues. ◼ Shifts in this pressure range happen on the flat portion of the curve. Clinical Application (cont.) ◼ The problem is a Change on the STEEP portion of the curve Right Shifts - Loading O2 in the Lungs Asthmatic with acute exacerbation ◼ PAO2 of 60 mmHg. ◼ PcO2 = 60 mmHg = HbO2 90% as it leaves the alveoli. ◼ If curve shifts to the R (pH:7.1)= HbO2 will be only 75% with the same 60 mmHg. Total O2 delivery may be lower than what is indicated by the PaO2. If R shift is accompanied by decreased cardiac output or reduced Hb, ability to transport O2 will be jeopardized even more. Right Shifts - Unloading O2 at the Tissues ◼ If tissue cells metabolize 5 vol% of O2 when O2 dissociation curve is in normal position, plasma PO2 must fall from 60 mmHg (HbO2 90%) to about 35 mmHg to free 5 vol% of O2 from the Hb. ◼ If curve shifts to the R (pH 7.1 – HbO2 75%) = PO2 at the tissues would only have to fall from 60 mmHg to about 40 mmHg to unload the same 5 vol%. Left Shifts - Loading O2 in the Lungs Asthmatic with acute exacerbation ◼ PAO2 of 60 mmHg. ◼ PcO2 = 60 mmHg = HbO2 90% as it leaves the alveoli. ◼ If curve shifts to the L (pH:7.6)= HbO2 will be 95% with the same 60 mmHg. Left Shifts - Unloading O2 at the Tissues ◼ If tissue cells metabolize 5 vol% of O2 when O2 dissociation curve is in normal position, plasma PO2 must fall from 60 mmHg (HbO2 95%) to about 35 mmHg to free 5 vol% of O2 from the Hb. ◼ If curve shifts to the L (pH 7.6 – HbO2 95%) = PO2 at the tissues would have to fall from 60 mmHg to about 30 mmHg to unload the same 5 vol%.