Lecture 6: Hemoglobin Saturation

saturation of hemoglobin

1. Saturation of hemoglobin is a measure of how much oxygen is bound to hemoglobin
a. 100% saturation all 4 binding sites on every hemoglobin have oxygen bound to them
2. as more oxygen bind, it increases affinity for more to bind ---> increase saturation of hemoglobin

T or F: when oxygen binds to hemoglobin, oxygen affinity for that protein increases

True

When blood arrives to tissues HbO2 is...

100%

when blood leaves tissues: HbO2 is...

78%

Gas exchange affecting oxyhemoglobin dissociation curve, RT shift...

promotes O2 unloading, decrease O2 affinity

Gas exchange affecting oxyhemoglobin dissociation curve, LT shift...

oxygen loading, increase oxygen affinity

what factors affect gas exchange?

-PO2 ambient
-temp
-ambient pH
-BPG

PO2 ambient

-active tissue consumes oxygen rapidly
-at low PO2 ---> HbO2 releases more oxygen

Temperature

increase in T ---> shift to RT (promote oxygen unloading)

ambient pH

active tissues release more CO2 ---> lower pH
Bohr Effect

BPG

RBC's use anaerobic respiration
-BPG is metabolic intermediates
-works to stabilize deoxyhemoglobin to reduce oxygen affinity

Things that stimulate production of BPG

Fever
T4
GH
T
Epi