Respiratory Physiology Flashcards
respiratory pigments
- oxygen transport pigments
- serve to bind O2 at respiratory surface and transport it through blood to tissues, and to remove CO2
- some also used as storage (ex: myoglobin in tissues)
- reversible combination with oxygen (pick up O2 at lungs, release at tissue)
inc the amount of O2 that can be carried by unit volume of blood
facultative diffusion
accepts O2 from hemoglobin and stores it in tissues until muscle need it
hemoglobin
- acid-base buffers
- participate in blood CO2 transport and O2 transport
- each contains 4 iron porphyrin prosthetic groups (hemes)
- contains 2 copies of alpha globin and 2 copies of beta globin
- each 4 polypeptide chains contain a heme molecule which is site for O2 binding
heme
associated non-covalently with protein globulin
- each heme binds 1 oxygen (4 hemes)
- 4 units=4 O2 molecules
globins
- proteinaceous
- subunits are different
human fetal hemoglobin
gamma and epsilon chains
oxygenated
hemoglobin combined with O2
deoxygenated
hemoglobin released O2
differences in Hb are due to differences in…
- amino acids in proteins
- alpha globin genes from chromosome 16
- beta and fetal genes from chromosome 11
where is hemoglobin found?
inside RBC (except with some insects)
myoglobin
- muscle hemoglobin
- 1 heme
- concentrated in muscle (cytoplasm of muscle fibers)
- hemoglobin unloads oxygen to myoglobin
- myoglobin has greater oxygen affinity than hemoglobin
chlorocruorin
- “green hemoglobin”
- 80 hemes per molecule
- green, found in 4 families marine annelids
- free floating, not specialized cells (dissolved in blood plasma)
- contains Fe and heme
- binds 1 O2 molecule per heme
hemerythrin
- 8 subunits
- no heme
- contain Fe directly to protein (each O2 binding site has 2 iron atoms)
- found in polychaetas
- sound in blood cells
hemocyanin
- copper containing pigment bound directly to protein (each O2 binding site has 2 copper atoms– 1 O2 per 2 Cu)
- no heme, no iron
- blue with oxygen
- high mw keeps down osmolarity
- not found in blood cells
- found in non-insect arthropods
- reverse Bohr effect (dec pH-> inc affinity)
never in muscle/solid tissue)
cytochromes
- have heme structure
- involved in electron transport and oxidative phosphorylation in mitochondria
Affinity for Oxygen
- affinity= how readily combine with O2
- respiratory pigments combine reversibly with oxygen over a range of partial pressures of O2
- thus serving as O2 carriers by loading at the respiratory surface and unloading at the tissues
saturated
O2 partial pressure is high enough for all O2 binding sites to be oxygenated
% saturation
percentage of binding sites that are oxygenated
Hb-O2 saturation curve
shows the relation between the percentage of binding sites that are oxygenated and the O2 partial pressure
P50
- when Hb is 50% saturated
- partial pressure of O2 at 50% saturation of hemoglobin
- measure of affinity of a particular Hb for O2
as P50 inc-> affinity dec
low affinity
pigments that need high O2 partial pressure for full loading and unload substantial amounts of O2 at high partial pressures
high affinity
pigments that load fully at low partial pressure and require low partial pressure for unloading
a shift to the right means…
O2 affinity
the O2 partial pressure needed to saturate is higher and the P50 is higher, thus… O2 affinity is lower
(lowering O2 affinity shifts to the right, raising affinity shifts to the left)
When hemoglobin molecule binds 1 O2…
this increases affinity of the molecule to bind more O2
- if 4 hemes bind O2 = 100% saturated
- the affinity of Hb must be turned to specific needs of the organism (ie: animals need to bind Hb at the lungs and unload it at the tissues; partial pressure of O2 differs at these two sites)
best strategy
- animals try to have 90-95% saturation at lungs, while still being able to unload at tissues, where there’s low PO2 at capillaries
- hemoglobin with high affinity are saturated at low partial pressures of O2 (es: myoglobin)
- hemoglobin with great O2 affinities facilitates movement of O2 into blood from the environment because O2 is bound to hemoglobin at low PO2
- since tissues have low PO2, you don’t want to have great affinity here, because you want hemoglobin to release oxygen at tissues
- hemoglobin is nearly saturated at O2 partial pressures maintained in lungs by breathing
what types of respiratory pigments have greater oxygen affinity than hemoglobin
- myoglobin has greater oxygen affinity then hemoglobin
- fetal hemoglobin has greater oxygen affinity than adult hemoglobin
- in both cases, this facilitates hemoglobin unloading oxygen to myoglobin/fetal hemoglobin
- with lower affinity it won’t bind O2 at low PO2 (at tissue), so hemoglobin unloads more to these other pigments
- hemoglobin with greater O2 affinity will not release O2 to tissues until PO2 is very low
fish P50
lesser P50, greater affinities than mammals, so it can uptake O2 in more oxygen deprived environments
bird P50
- have greater P50, lesser affinities than mammals so it can unload more
- with high MR, they need great O2 at tissues
- p50= 40-60 mmHg
main point about hemoglobin
- hemoglobin with great O2 affinity favors uptake of O2 by blood
- hemoglobin with less O2 affinity favors release of O2 to tissues
**Hemoglobin should have great affinity at respiratory surface and low affinity at tissues
bicarb equation
CO2 + H2O <-> H2CO3 <-> H+ + HCO3-
- high CO2 shifts equation to right-> high H+, low pH
- increase in H+ shifts equation below to left-> dec O2 affinity
- deoxyHHb <-> H+ + Hb
HHb+ + O2 <->HbO2 (oxyHb) + H+
Bohr effect
- inc CO2-> dec affinity by dec pH
- H+ complexing with Hb and releasing O2
- also CO2 complexes with Hb and releases O2
- shifts Hb dissociation curve to right
- at low pH and high PCO2-> dec affinity and dec P50
- normally occurs when blood enters capillaries because of increased pCO2
at tissues…
pH, pCO2, affinity, P50
- low pH, high pCO2, low affinity, high P50
- low pH and high PCO2 allows hemoglobin to unload more O2
stagnant water
low pH and high pCO2 causes problems with animals loading at respiratory surfaces
inc in CO2 partial pressure
causes pH decrease
inc in H+ concentration
inc in combination os Hb with H+-> favors dissociation of O2
what is responsible for Bohr effect?
- Proteins come from:
1) COOH terminal of the beta chain has a histidine (N+) imidazole group
2) amino terminal of the alpha chain has NH3 - some fish won’t show Bohr effect
Reverse Bohr effect
- animals with hemocyanin have a reverse Bohr effect
- ie: dec pH-> inc affinity
- good for animals that live in stagnant waters
- also back up hemoglobins found
- fishhave Hb with a Bohr effect (facilitates unloading at tissues) and also one without a Bohr effect (facilitates loading at the respiratory surface)
Root Effect
- inc in CO2 partial pressure/dec in pH causes Bohr effect AND reduces amount of O2 the respiratory pigments bind when saturated
- dec pH-> dec amount of O2 bound to Hb (dec in O2 capacity
- root effect at low pH: blood can’t bind O2 at respiratory surface
- acidification forces O2 bound to hemoglobin to dissociate by change og pH
2,3 DPG
- in RBC
- Inc in 2,3 DPG-> dec affinity, inc P50, facilitates O2 unloading
- IHP in birds
- ATP in fish and some amphibians
temperature and Hb
- increased temperature shifts Hb-O2 dissociation curve to the right
(dec affinity=inc P50, low temp=inc affinity) - O2 affinity of respiratory pigments is inversely dependent on temperature
what do P50 values depend on
- pH, pCO2, 2,3 BPG, and temperature
in general with mammals…
P50/affinity trend
small mammals have greater P50s than large ones
- with greater MR, they need more O2 to tissues
O2 affinity of blood hemoglobin tends to decrease as body size decreases
- need lowest affinity possible so its just saturated at respiratory surface and can unload at tissues
P50 values
- normal range: 20-45
- adult human: 30 (2 alpha, 2 beta)
- fetus: 20 (fetal Hb has greater affinity; 2 alpha, 2 gamma–> allows fetal Hb to take up O2 from mother because O2 leaves lower affinity hemoglobin of mom to go to higher affinity hemoglobin of fetus)
Reptile P50
- great diversity, meets needs of organism
- P50- 20-50
amphibian P50
- tadpoles: low P50s, high affinity because of water
- Adults: higher P50s
fish affinity
fast swimmers, stagnant warer, low O2
- fast swimmersL from water with high Po2 and low temp; usually have Hb-O2 curves to right of other fish (lower affinity helps unload O2, thy don’t need high affinity in high O2 tension water)
- stagnant water fish: low P50s
- species that live in low O2 environment have evolved respiratory pigments with higher O2 affinities than related species in high O2 environments
Invertebrate P50s
- respiratory pigments in blood of some invertebrates probably functions as O2 stores
- very high O2 affinity (do not unload under routine conditions)
- unload when face severe O2 shortages
effect of temperature on Hb (fish)
1) increased temp-> dec O2 concentration of water
- elevated temps create O2 stress
2) high temp-> inc MR of poikilotherms (require more O2 at elevated temp; may also result in inc PCO2 levels and lower pH-> dec affinity and higher P50s)
3) high temp-> inc P50, dec affinity, dec amount absorbed at respiratory surface
means of compensation
1) inc ventilation (ie: inc respiratory rate to get more O2, also may inc loss of CO2-> inc pH and inc affinity; yet inc muscle activity and energy costs)
2) inc blood flow across respiratory surface to maintain high O2 gradient
3) increased Hb concentration and/or number of RBC (more RBC in oxygen poor environment; in environment without O2-> 20x increase in Hb concentration)
4) change in type of Hb (ex: summer Hb has higher affinity; synthesizing different molecular forms(diff globulin-> different O2 affinity)
5) some sort of modulation with Hb
6) back up Hb
several invertebrates and some vertebrates lack respiratory pigments
- no O2 transport by blood hemoglobin
- no Hb, clear blood, only serum
- Active fish, MR high
- high rate os blood circulation, high CO, high blood volume
- large hearts circulate blood rapidly
- very high respiratory surface area where O2 can diffuse
- important that cold water has greatest O2 tension