Blood Gases and Transport Flashcards
What is cooperativity for hemoglobin?
the binding of one O2 increases the binding affinity of the other O2, 1 O2 coming off decreases the affinity of the other O2 binding the hemoglobin
What factors affect oxygen binding and release on hemoglobin?
oxygen tension, pH, pCO2, 2,3-BPG, and temperature
How does oxygen tension affect oxygen binding and release with hemoglobin?
it is high in the lungs and low in the tissues; drives the O2 on near the lungs and off near the tissues
How does pH affect O2 binding and release with hemoglobin?
acidity enhances the release of O2, lowering pH shifts oxygen dissociation curve to the right so O2 affinity is decreased
How does pCO2 affect O2 binding and release with hemoglobin?
increasing the concentration of CO2 at constant pH lowers oxygen affinity of Hb
How does 2,3-BPG affect O2 binding and release with hemoglobin?
2,3-BPG can bind to and stabilize deoxyhemoglobin lowering Hb affinity for oxygen, shift in the O2 sat curve to the right
How does temperature affect O2 binding and release with hemoglobin?
increase in temperature lowers Hb affinity for O2, exercise increases temp which helps O2 delivery to tissues
What causes BPG to accumulate at higher concentrations in the body?
acclimatization to high altitudes, chronic lung disease, anemia, right to left cardiac shunt, congenital heart disease, and pulmonary vascular disease, causing a decrease in oxygen affinity
How is fetal hemoglobin oxygen affinity compared to adult hemoglobin?
leftward shift because of gamma instead of beta chains, gamma lacks the two positively charged groups needed to bind 2,3-BPG and has a tighter association with O2
Why does fetal hemoglobin need to have a higher O2 affinity? What is the downside?
need to compete with mom’s hemoglobin so they get O2 in the placenta to take to their tissues, it is harder to offload to fetal tissues
What is the binging affinity of myoglobin compared to hemoglobin? Why is this important?
greater affinity, so under conditions of oxygen deprivation myoglobin will release O2, also necessary so when oxygen is rich it will be taken up to the myoglobin over the hemoglobin so it will be available for oxygen deprived situations
How does anemia effect O2 carrying capacity?
decreases O2 carrying capacity without altering P50 of blood, maintains saturation
How does polycythemia effect carrying capacity?
increase O2 capacity without altering P50, maintain saturation
How does carbon monoxide affect O2 carrying capacity?
binds to heme 200x greater affinity than O2, eliminate cooperative effect of oxygen binding to Hb
What is methemoglobin?
oxidation of heme iron from ferrous (Fe++) to ferric (Fe+++) results in methemoglobin, which is unable to release O2
What enzyme converts methemoglobin back to normal hemoglobin?
NADH-methemoglobin reductase (diaphorase I)
What is methemoglobinemia?
results from agents that oxidize ferrous ion, presence of abnormal hemoglobins, reduction in the ability to reduce heme ferric ions, or a combination; levels of 50% or greater= seizures or death; treat with reducing agents like methylene blue, also called hemoglobin M disease
What is the Bohr effect?
when oxygen binds to hemoglobin, protons are dissociated from histidine residues, and increase in H ions drives reaction to promote release of oxygen from Hb; decreased pH is associated with oxygen demand; increased metabolic rate results in increased production of CO2 and lactic acid and they promote the release of oxygen from Hb
What are the major forms of transport for CO2?
dissolved CO2, HCO3 formed by ionization of H2CO3 produced from CO2 and H2O catalyzed by Carbonic anhydrase, and attached to protein as carbamino groups mainly on the N-terminal amino group of deoxyhemoglobin which has a higher affinity for CO2 than oxyhemoglobin
What is the chloride shift?
bicarbonate-chloride carrier protein in erythrocyte membrane shuttles Cl and HCO3 in opposite directions; in the lungs HCO3 migrates into the cells to be converted to CO2 for exhalation and Cl returns to plasma
In what two ways does the binding of O2 displace CO2 from hemoglobin?
Haldane effect, release of hydrogen
What is the Haldane effect?
when O2 binds to Hb, Hb has a reduced ability to bind CO2 as carbamino hemoglobin and CO2 is released
Other than the Haldane effect how does O2 binding to Hb help offload CO2?
when O2 binds to Hb hydrogen is released and they turn and bind to HCO3 which dissociates to H2O and CO2. CO2 is released from the blood into alveoli to be expired
What percent of CO2 transported back to the lungs is in the form of CO2, Hb-CO2, and HCO3?
CO2= 10%, Hb-CO2= 30%, HCO3= 60%