Respiration: Oxygen Transport Flashcards
oxygen transport cascade (5)
- ventilation (air)
- pulmonary diffusion (lungs)
- circulatory diffusion (blood)
- muscle diffusion (capillaries)
- muscle utilization (tissues)
how does PO2 and PCO2 change from the environment to the tissues (2)
- PO2 decreases from environment to the tissues
- PCO2 decreases from the tissue to the environment
solubility of O2 in aqueous fluids
- low
metalloproteins/respiratory pigments
- proteins containing metal ions which reversibly bind to oxygen
how do respiratory pigments affect oxygen carrying capacity
- increase O2 carrying capacity by 50-fold
respiratory pigments: types (3)
- hemocyanins
- hemerythrins
- hemoglobins
respiratory pigments: hemocyanins
- organisms
- metal type
- location
- appearance
- arthropods and molluscs
- contain copper
- usually dissolved in hemolymph
- appears blue when oxygenated
respiratory pigments: hemerythrins
- organisms
- metal type
- location
- appearance
- worm-like organisms and sea clams
- contains iron directly bound to protein
- usually found inside coelomic cells
- appears violet-pink when oxygenated
respiratory pigments: hemoglobin
- organisms
- metal type
- location
- appearance
- vertebrates, nematodes, crustaceans, insects
- globin protein bound to heme molecule containing iron
- encapsulated in RBCs
- appears bright red when oxygenated
hemoglobin structure (2)
- structure (2)
- mutations
- often 2 alpha and 2 beta chains
- each chain is ~145 amino acids
- single aa substitutions can have profound effects on function
myoglobulin
- type of hemoglobin found in muscles
what percentage of blood are RBCs
- 30-60% of blood consists of RBCs
Hb and RBCs
- RBCs encapsulate Hb and transport O2 and CO2
- allows for fine-tuning of micro-environment around Hb to optimize function
what is the percentage of physically dissolved O2 and O2 bound to Hb in blood (2)
- 1.5% of O2 is physically dissolved
- 98.5% of O2 is bound to Hb
oxygen equilibrium curve (OEC)
- compares percent saturation of hemoglobin with PO2
OEC: shape (2)
- sigmoid shape
- allows for maximal unloading with a small change in PO2
OEC: maximal unloading (2)
- occurs at 50% O2 saturation of Hb (P50)
- animals alter P50 of hemoglobin to optimize O2 loading and unloading
how does the circulatory system respond to O2 stress (exercise, hypoxia, diving) (2)
- RBCs are released from the spleen
- elevates hematocrit and hemoglobin levels
releasing additional RBCs from spleen: advantage (2)
- enhance oxygen uptake and delivery
- increase O2 carrying capacity in blood
releasing additional RBCs from spleed: disadvantage
- viscosity of blood will eventually be too high, decreasing flow of blood
hemoglobin molecule stages (3)
- T state
- R state
- Hb molecule goes from T state to R state as it is oxygenated
Hb: T state (2)
- tense state
- oxygenation of the Hb is difficult
Hb: R state (2)
- relaxed state
- O2 can be added to the Hb more easily
T –> R state transition (2)
- transition is associated with weakening/breaking of salt bridges within Hb molecule
- binding of each additional O2 induces a conformational change that relaxes Hb further
what are the ideal OEC conditions at the gas exchange surface (2)
- high Hb affinity (low P50) maximizes O2 uptake
- left-shifted OEC
what is the ideal OEC conditions at the tissues (2)
- low affinity Hb (high P50) maximizes tissue O2 delivery
- right-shifted OEC
how does “right shifting” the OEC affect respiration (2)
- P50 is increased
- facilitates O2 delivery to active tissues producing CO2
how does “left shifting” the OEC affect respiration
- P50 is decreased
- facilitates O2 uptake at the respiratory surface