# Hemoglobin Tetramer [Hb(O 2 )] [Hb]P O 2 K 2 = [Hb(O 2 )] [Hb]P O 2 K 3 = [Hb(O 2 )] [Hb]P O 2 K 4 = [Hb(O 2 )] [Hb]P O 2 K 1 = = 4.88 = 15.4 = 6.49 =

Dec 21, 2015

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#### hyperbolic binding o

• Slide 1
• Hemoglobin Tetramer [Hb(O 2 )] [Hb]P O 2 K 2 = [Hb(O 2 )] [Hb]P O 2 K 3 = [Hb(O 2 )] [Hb]P O 2 K 4 = [Hb(O 2 )] [Hb]P O 2 K 1 = = 4.88 = 15.4 = 6.49 = 1750 Whole blood can carry as much as 0.01 moles of O 2. Plasma can carry only 0.0001 moles of O 2 Hb (aq) + O 2(g) Hb(O 2 ) (aq) Hb(O 2 ) (aq) + O 2(g) Hb(O 2 ) 2(aq) Hb(O 2 ) 2(aq) + O 2(g) Hb(O 2 ) 3(aq) Hb(O 2 ) 3(aq) + O 2(g) Hb(O 2 ) 4(aq)
• Slide 2
• Slide 3
• Slide 4
• Myoglobin Tetramer [Mb(O 2 )] [Mb]P O 2 K = = 271 Mb (aq) + O 2(g) Mb(O 2 ) (aq) Change the partial pressure of O 2 will shift the equilibrium. Increasing P O 2 will shift the equilibrium to the right, decreasing P O 2 will shift the equilibria to the left.
• Slide 5
• Myoglobin Higher affinity for O 2 (low P O 2 ) Hyperbolic binding O 2 :Mb 1:1 Binds O 2 in tissues Hemoglobin Lower affinity for O 2 (High P O 2 ) sigmoidal binding O 2 :Hb 4:1 Binds O 2 in lungs, releases in tissues At a P O 2 of 0.13 atm both hemoglobin and myoglobin are 95% saturated. With a P O 2 of 0.040 atm hemoglobin is only 55% saturated whereas myoglobin is above 90%. Thus, as P O 2 decreases in the capillaries hemoglobin releases almost half Of the O 2 which O 2 poor myoglobin can pick up.
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