RS Lec 6 Flashcards
(46 cards)
O2 in blood forms
- dissolved (2%)
- combined with hemoglobin (98%)
dissolved O2 proportional to (2)
PO2
solubility
98% (197 ml/L) of O2 carried on
hemoglobin in red blood cells
hemoglobin made of
- globins: 4 subunits (a.a) - 2 alpha/ 2 beta
- 4 heme groups
heme (def.)
porphyrin ring structure that has Fe2+ that O2 binds
each HB molecule can bind
4 O2- one per subunit (O2 + Hb HbO2)
Hb
deoxyhemoglobin
HbO2
oxyhemoglobin
O2 capacity
max amount of O2 that is combined with Hb
1 g Hb combines with (amount of O2)
1.39 ml O2
normal conditions (g Hb/ 100 ml blood)
15g Hb/100 ml
max O2 capacity (g Hb/100 ml)
20.8 ml O2/100 ml blood
Hb saturation
- percentage of available Hb binding sites that have O2 attached
- O2 with Hb/ O2 capacity x 100%
Hb saturation of arterial blood (100 mmHg PO2)
97.5%
Hb saturation of mixed venous blood (40 mmHg PO2)
75%
factors that determine Hb saturation
- arterial PO2 (most important)
- cooperative binding (sigmoidal dissociation curve)
dissociation curve sensitive to
- pH
- pCO2
- temp.
cooperative binding
O2 binding causes change from T (tense) to R (relaxed) state in a globin, facilitates change in other globin and additional O2 binding
plateau in dissociation curve
60-100 mmHg
plateau in dissociation curve can indicate
reduced arterial PO2 (therefore reduced alveolar PO2
plateau in dissociation curve (saturation drop)
10 % over 100 to 60 mmHg of PO2
steep portion in dissociation curve
40 - 60 mmHg
steep portion in dissociation curve unload
large amounts of oxygen with small decrease in PO2
steep portion in dissociation curve changes leads to
changes in O2 unloading by the binding of compounds produced in peripheral tissue