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img028 - leftward shift also indicates that oxygen is...

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Unformatted text preview: leftward shift also indicates that oxygen is loaded more easily onto hemoglobin. Under normal conditions 3 P02 of around 45 mmHg produces 80% saturation of hemoglobin. With a rightward shift, at P02 of greater than 45 mm Hg is required to produce the same 80% saturation; with a leftward, at P02 of less than 45 mm Hg produces 80% saturation. Wan-y 5mm: Guam import it warm wummoth 8 i l Tun-m i é * As hloudmvolstolungsileools- increasing afl‘inity for 02 5““ °“""°“““" Click Temperature: see more: Temperature ametwmdm Mowtozunwmcnml Result: more 02 is unloaded in theue that is highly active 9 n I. I too 'qlflnll Elke! at pH * mmdwmmwmm mehu-qu-Bomafieer * Pocahamdmhauusafimytovum- Whmmm *zummmmmrmmm orymmcyhs.M5mOzswplyhhMZ.S—DPG mmnydmofloblnknom. * manwmmmm afl’ects the affinity of hemoglobin for oxygen by altering the structure of the hemoglobin molecule. This structural change has important functional consequences — it decreases the hernoglobin’s affinity for oxygen. As a result more 02 is unloaded in tissue that is highly active. As blood travels back to the lungs its temperature decreases in increases its afi'mity for 02 in the lungs. Click the Back Button: Click pH see more: The efi‘ectnfigflpn the hemoglobin-oxygen dissociation curve is known as the Bohr efl‘ect, which is based on the fact that when oggen binds to hemoglobin certain amino acids in the protein release hydrogen ions. An increase in H ion concentration (a decreaue in pH) pushes the reaction to the left, causing some oxygen to dissociate from the hemoglobin even when P02 is kept constant. The hydrogen ion concentration tends to increase in active tissue and this facilitates oxygen unloading. Click the Back Button. Click PC01 see more: C02 reacts reversibly with certain amino groups in hemoglobin to form carbamiuohemoglobin (HbCOz). When C02 is bound to hemoglobin it changes hemoglobin’s confonnation and decreases its affinity for oxygen. —- this is known as the earbamino effect. This is one way C02 is msported in the blood. 2,3 diphosphoglycerate is a chemienl compound produces in erthrocytes from an intermediate compound in glycolysis, the anaerobic pathway by which erythrocytes obtain all their energy. When oxyhernoglobin is present in high concentrations it inhibits the enzyme that forms 2,3, DPG. If oxyhemoglobin levels are low (i.e. when 02 supplies are limited, then 2,3 DPG synthesis occurs and enhances the unloading of oxygen in the respiring tissues that need it. — Anemia and high altitude. Click Back button. Click the Home Menu Button ‘ You have now completed this module l . ...
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