lecture 13,14- Flashcards
(35 cards)
The functions of the mamallian respiratory system ?
- Provides O2 to blood and eliminate CO2 from blood
- regulates blood H+ conc
- Forms speech sounds
- defends against inhaled microbes
- Traps & dissolves blood clots arising from systemic veins
highly branched airways=alveoli->site of gas exchange
What are the 2 circuits that are in circulatory system ?
- Pulmonary circulation:right ventricle->lungs->left atrium
- Systemic Circulation:left ventricle ->peripheral organs & tissues->right atrium
delivery of nutrients & O2 to tissues& removal of CO2
BC suspended in plasma
Where are RBC produced ?
prod in red bone marrow -destroyed in spleen & liver
-hormone : erythopoietin
formation requires iron,folic acid,vitamin B12
What is anaemia ?
decrease in the ability of blood to carry O2
1. A decrease in total no of RBC
2. lower conc of Hb per RBC
3. or combo of both
4. bone marrow failure
5.
ron storage in body: 50% (of total body iron)
is in haemoglobin, 25% in other haem/heme-
containing proteins (e.g. cytochromes) in
cells, and 25% in liver as ferritin (protein
RBC and the transport of respiratory gases ?
blood within pulmonary capillaries seperated from air
by thin barrier
Total alveolar SA is huge–>rapid exchange of large quantities of O2 & CO2 by diffusion
Blood transport of respiratory gases ?
Vertebrates use haemoglobin in RBCs; high concentration
of haemoglobin (in mammalian blood) allows each volume
of blood to carry 50-60x more O2..!
Haemoglobin the respiratory pigment ?
Quaternary structure
composed of more than 1 polypeptide chain together
Vertebrate Hb has 4 polpeptide globin subunits
2 a,2b subunits
each heme= 1 Fe2+ atom reversibly bind to1 O2
What is Hb positive cooperativity ?
ability to combine with O2 depends on PO2
High PO2 –>can carry 4 O2 max
Low PO2 –>some O2 is released from Hb
displayed by hB binding dissociation curve
Sigmodial :low PO2 ,only 1 subunitbinds to 1 O2–>conformational change ->altering quaternary structure–>increasing affinity of other subunits
easier for 2nd O2 to bind
some extra info on Hb and CO ?
combine with other ligands -H+,CO2
allosteric ligands/modulators
CO binds with 240 fold higher affinity than O2 competing with the latter–>preventing O2 being transported -toxic /deadly at high conc
Total amount of O2 trnasported by blood Hb
What is normal partial pressure of gas in air and body ?
Alveolar PO2 is lower than atmosphere PO2 because of net diffusion of alveolar O2 into lung capillaries
Alveolar Po2 and PCO2 determine the sytemic arterial PO2 , PCO2
Hb abilty for loading & unloading O2 ?
High PO2 in lungs vs Low PO2 in venous blood–>Hb binds (loads O2)
Low PO2 in tissues cappilaries vs High PO2 in arterial blood
Loading:oxygenation of Hb
Unloading :deoxygenation
How does Hb load O2 in the lungs ?
Plasma & RBC enetering (venous blood) have PO2 of 40mmHg
O2 diffuses into blood–>RBC
O2 binds Hb removing O2 from dissolved solution –> lowers the plasma PO2
thuis gradient is maintained unitl Hb is 100% saturated
Exiting blood :100mmHg
O2 bound to Hb does not contribute directly
to blood PO2; only dissolved O2 does
What is Hbs loading plateau O2 ?
loading plate provides protection
If alveolar PO2 falls to 60 mmHg
even a moderate limitation of lung
function still allows for significant Hb saturation!
Hb:O2 unloading in tissues ?
Plasma and RBC entering tissue capillaries =PO2 -100 mmHg
O2 unloaded into blood-then diffuses into tissue/cells
plasma PO2 falls-only 25% O2 is unloaded
exiting blood PO2 -40mHg
O2 unloading in general ?
cells still can get more O2 whenever they increase activity
Exercising muscle -consumes more O2 –>lowering intracellular & interstitial PO2 –>increasing blood-to-cell ratio
-increased rate of O2 diffusion from blood into cells=decrease in RBC PO2 casues additional unloading
if tissue PO2 fall below 40mmHg-reserve O2 released
Myoglobin and properties ?
muscle cells -own O2 binding aka myoglobin
found in skeletal & cardiac muscles
consists of 1 polypeptide chain with 1 heme
can bind to 1 O2 with very high affinity
1. facilitates diffusion of O2 in muscle cell
2. provides O2 reserve
Myoglobin as a reserve of O2 how does it work ?
during exercise=high metabolic demand & interruptions in supply of O2 :
tissue PO2 drops and Hb cant supply more O2 -myoglobin then release its bound to O2
Myoglobin abindant in muscles of diving muscles
During vigorous exercise, blood PO2 is lower than at rest → blood passes through lungs
faster:↓ time of gas exchange
Human Hb vs Human Mb O2 eqm curves ?
Myo=hyperbolic O2 eqm curve contains 1O2 binding sites per molecules ->no coperativity
Is Hbs affinity for O2 variable ?
yes its dependent on
1. CHemical composition of Hb
2. presence of 2,3-bisphosphoglyceric acid
3. pH,CO2,H+
4. Temperature
What is the chemical composition of Hb ?
Fetal Hb:8 weeks after conception consists of 2 a,2y globin subunits
higher affinity for O2 than adult Hb
Adult Hb :consists of 2a2b globin subunits
How does living at higher altitiudes affect Hb ?
Llamas-live at >5000 metres above seaw level
higher affinity for O2 than fetal/adult Hb
Hb becomes saturated at much lower PO2
Llama vs Human ?
Llama
* Hb with high affinity for O2
* binding curve shifted to left
* saturated occurs at lower PO2 values
* tissues can operate at lower PO2
Human
* Hb never 100% saturated due to low environmental PO2
* binding curve shifted to right
* More O2 is unloaded in tissues
What does the presence of 2,3-bisphosphoglyceric acid do ?
reversibly bind to Hb –>alosteric conformational change
–>reduces Hb affinity for O2
High levels of 2,3-DPG in mature RBCs as they
rely on glycolysis (there are no mitochondria):
↑ [2,3-DPG] enhances O2 unloading.
What is the Bohr effect ?
O2 affintiy decreases as pH decreases so curve shifts to right.