Exam 4: Respiratory L4 Flashcards
Oxygen Transport in the Blood:
Oxygen is carried in the blood in two forms:
1.
2.
Oxygen is carried in the blood in two forms
- Dissolved
- Bound to Hemoglobin
Dissolved Oxygen:
- Measured clinically as ______
- Amount that can be dissolved follows ____ Law
- Per 1 mmHg of PO2 —–> ______ mL 02/100 mL blood
- normal blood —–> ____ mL O2/ 100 mL blood
Dissolved Oxygen:
- measured clinically as PaO2 (blood gas analysis)
- amount that can be dissolved follows henry’s law (concentration of solute in gas is directly proportional to partial pressure)
- Per 1 mmHg of PO2 —> 0.003 mL O2 per 100 mL blood
- normal blood has 0.3 mL O2/ 100 mL
How much oxygen do we use per minute in the blood?
How much of that does dissolved O2 provide?
Normal O2 consumption is roughly 250 mL O2/min
Dissolved gives us 15 mL of O2 per minute
(dissolved O2 is not enough)
Dissolved Oxygen:
- ______ percentage of total O2
- Under normal conditions it is _____
Calculation sample question: What is the PAO2 if you breathe 100% oxygen and the PAco2 is 45 mmHg (R = 0.8)
Dissolved Oxygen:
- SMALL percentage of total O2 in blood
- Under normal conditions its almost negligible
Final answer: 657 mmHg
Hemoglobin:
How many heme groups are there?
How many polypeptide chains? Which kind?
What is adult hemoglobin vs fetal hemoglobin
The binding/dissociation of O2 occurs in ____ and changes ______
Hemoglobin:
4 heme groups containing iron (this is where oxygen binds)
There are four polypeptide chains (2 alpha and two beta), this is for HbA
For kids less than a year old, HbF has 2 alpha globin and 2 gamma globin chains
The binding/dissociation of O2 occurs in milliseconds and changes light absorption of Hb (red means oxygenated, blue means deoxy)
Explain the two states of Hb related to O2 binding
Explain O2 binding on heme
Hb has two states, tense and relaxed
Tense State (T) : no oxygen bound, low affinity for O2
Relaxed State (R): oxygen bound, high affinity
Oxygen binding is reversible, and also the oxygen binding on Hb is cooperative (sigmoidal curve)
That means the likelihood of oxygen binding goes up with each oxygen bound
How much Hb is bound to oxygen within the normal range of PO2 ? Draw the oxygen dissociation curve to help.
What is the normal unloading of oxygen by hemoglobin (in mL O2 per 100 mL blood)
Most Hb is oxygen bound within the range of normal PO2 .
Curve is shown in attached picture.
Normal unloading is approx 4.5 mL O2 per 100mL
Oxyhemoglobin Dissociation Curve:
At PO2 > 60 mmHg what are the changes in Hb saturation
(what does that mean at those pressures)
At PO2 < 60 mmHg : small changes in pressures lead to _____
(what does that mean?)
At PO2 > 60 mmHg , small canges in Hb saturation (loading and transport at these pressures… facilitates normal oxygen transport to organs/cells)
At PO2 < 60 mmHg: small changes in pressure lead to release of large amounts of O2
(facilitates release of oxygen to organs and cells)
The oxyhemoglobin saturation curve is NOT static.
The curve responds to the local enviornment to ______
Explain what a right ward vs leftward shift means
Also explain P50 and how that is effected by left or rightward shift
The oxyhemoglobin saturation curve is NOT static. The curve responds to the local enviornment to modulate loading and unloading.
P50 is the pressure at which 50% of the Hb are oxygen saturated
A left shift of the curve means an INCREASE in Hb-O2 binding (decrease in P50, meaning an increase in Hb O2 affinity)
A rightward shift of the curve means a DECREASE in Hb-O2 binding. (increase in P50, meaning Hb has a decrease in O2 affinity)
Explain which physiological factors cause a leftward shift of the Hb-O2 saturation curve
Explain which factors cause a rightward shift in the curve
Leftward Shift in the Curve (meaning increase in Hb-O2 affinity) : Decrease in temp, Decrease PCO2 , Decrease in 2,3-DPG, and a decrease in H+ ions (meaning increased pH)
Rightward Shift in the Curve (meaning decreased O2 affinity): Increased temp, Increased PCO2 , Increase in 2,3-DPG, Decrease in pH ( increase in H+ ions)
Explain the Bohr Effects on the Hb-O2 saturation curve
Bohr studied the effects of pH and PCo2 on the Hb-O2 saturation curve
An increase in pH (decrease in H+ ions) and a decrease in PCO2 causes a leftward shift of the curve (increased oxygen affinity)
A decrease in pH (increase in H+ ions), and an increase in PCO2 cause a rightward shift in the curve (decreased oxygen affinity)
Cheat code for hemoglobin oxygen saturation curve:
As X factor increases, Hb binding of oxygen ____
Just be aware of pH relationship to H+ ions
Cheat code:
As X factor increases, the Hb binding of oxygen decreases (shifts curve to the right)
(factors include temp, PCO2, 2,3-DPG, and H+ ions)
Just remember that decrease in pH means increase in H+ and vice versa
Metabolically active tissues will have an _____ in all of the factors, causing the dissociation curve to shift to the _____
Metabotically active tissues will have an increase in all of the factors, causing the dissociation curve to shift to the right and causing a decrease in the O2 affinity
Explain what happens to the hemoglobin oxygen saturation curve when the temperature drops vs rises
When the temperature drops, the curve shifts to the left, and oxygen affinity for Hb increases. Thus, not only does the blood get redistributed in cold weather, but also the blood that does get to the extremities does NOT unload its oxygen
When temperature rises, the sat curve gets shifted to the right, meaning more O2 is being unloaded in the tissues because the Hb o2 affinity decreased
What two factors constitute the Bohr Effect?
Bohr Effect: pH and CO2
The Bohr Effect: pH and CO2
What is hypercapnia?
How does CO2 react with Hb and affect O2 binding?
How does it compare to the effects of pH?
Hypercapnia = high CO2
CO2 does not directly compete for binding sites with O2. Instead, CO2 binds to amino groups and creates a carbamino Hb which decreases O2 binding
Therefore, high CO2 will shift the curve to the right, decreasing O2 affinity
The effects of CO2 are minor compared to pH
The Bohr Effect:
High CO2 leads to ____ pH
Respiratory acidosis ______ O2 affinity
Combo of both pH and CO2 constitutes the Bohr Effect: explain what needs to happen for a left or rightward shift
High CO2 leads to lower pH
Respiratory acidosis decreases O2 affinity
Bohr Effect:
low pH and high CO2 decreases Hb oxygen affinity and shifts the curve to the right
Higher pH and lower CO2 levels increase the HB O2 affinity and shifts curve to the left
2,3 DPG
Preferentially binds to ____
_____ affinity of Hb for oxygen (allosterically)
Increased DPG in _____ conditions
2,3 DPG preferentially binds to deoxygenated Hb
Decreases affinity of Hb for oxygen (allosterically)
Increase of DPG shifts curve to the right
There is Increased DPG in low oxygen conditions (where you want more oxygen dropped off)
Final RECAP on Hb-O2 saturation curves:
Explain what causes left ward vs rightward shift in the following conditions, and note how each shift affects affinity and P50
Temp
PCO2
2,3 DPG
pH
Leftward Shift: Increased Affinity (Decreased P50 )
- Decreased temp, decreased PCO2, decreased 2,3-DPG, and increase in pH (essentially a decrease in H+ ions)
Rightward shift: Decreased O2 affinity (increased P50)
- Increased temp, increased PCO2, increased 2,3-DPG, and decreased pH (increase in H+ ions)
Carbon Monoxide:
Hb affinity for CO is ______ than the affinity of O2
At 1 mmHg CO _____ binding sites are occupied
In the presence of CO: Hb affinity for O2 is ____, causing ________
What does the CO Hb saturation curve look like?
CO and Hb:
Hb has a 200x greater affinity for CO than O2
At 1 mmHg CO, ALL binding sites are occupied
In the presence of CO: Hb affinity for oxygen is ENHANCED, which prevents oxygen unloaded on the tissues
“it’s a double whammy”.. not only is CO going to bind and occupy the binding sites, but the O2 that stays bound will not be unloaded in the tissues either
Hb and CO:
CO binding “mimics” oxygen binding into the _____ state for _____oxygen affinity.
What does that mean for Hb O2 binding?
CO binding “mimics” oxygen binding into the relaxed state for enhanced oxygen affinity.
Hb not necessarily binding more O2 due to higher affinity, it’s just that the oxygen that is bound is less likely to unload/dissociate?
Sickle Cell:
Which form of Hb is it?
It is a ___ AA substitution in the ___ chain
It is normal with oxygen: it ____ at low oxygen
The sickle cell shape causes ___ and ___
Sickle Cell:
HbS
Single AA subsitution in the BETA chain
It is normal with oxygen; crystallizes at low oxygen
Sickle cell shape, hemolysis, anemia
Explain Hb within diabetes
Diabetes: Hemoglobin A1c
Increased blood glycose leads to increased cell glucose 6-P which increases the amount of glycosylated Hb
This glycosylation is irreversible. RBCs last for three months (120 days) so HbA1c gives an accurate 3 month running average of your blood glucose level
For PaO2, which level of partial pressure of oxygen in the arteries is hypoxia, and which level is in danger?
Give both the mmHg level and the o2 saturation percentage
PaO2 > 80 mmHg means HYPOXEMIA (97.5%)
PaO2 = 60 mmHg means DANGER (90%)
Altering Hb saturation is just as dangerous as altering your oxygen intake
How do you calculate the oxygen content in arterial blood…“CaO2”?
To calculate CaO2, you simply multiply O2 capacity by SO2.
1 g of Hb can bind to 1.34 mL of O2
That means at 100%, we have 20.1 mL O2/100 mLs
In order to calculate the oxygen content in arterial blood, you take the SpO2/SO2% as a decimal and multiply it by 20.1 mL O2/ 100mL