lecture_14 - Protein Function Globins and Antibodies...

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Protein Function Globins and Antibodies 3/12/2003
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Quaternary structure of deoxy- and oxyhemoglobin T-state R-state
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D-2,3-bisphosphoglycerate (BPG) C O O C C O PO 3 -- O PO 3 -- H H H BPD binds to hemoglobin and decreases the oxygen affinity and keeps it in the deoxy form. BPG binds 1:1 with a K=1x10 -5 M to the deoxy form but weakly to the oxy form
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BPG binds specifically to the deoxy state and stabilizes it in the T state. In the R state the central cavity is too narrow for BPG to fit or bind .
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The P50 value of stripped hemoglobin increases from 12 to 22 torr by 4.7 mM BPG
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At 100 torr or arterial blood, hemoglobin is 95% saturated At 30 torr or venous blood, hemoglobin is 55% saturated Hemoglobin releases 40% of its oxygen. In the absence of BPG, little oxygen is released. Between BPG, CO 2 , H + , and Cl - all O 2 binding is accounted for.
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BPG levels are partially responsible for High-Altitude adaptation
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BPG restores the 37% release of O 2 at higher elevations between arterial and venous blood
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lecture_14 - Protein Function Globins and Antibodies...

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