Animal Phys Ch 24

Front 1

Hemoglobin

Back 1

– Globin protein bound to a hememolecule containing iron

– Usually within blood cells

– Appears red when oxygenated

– Myoglobin is a type ofhemoglobin found in muscles

Front 2

Hemoglobin saturation in lungs and tissues- Partial pressures in mmhg needed for % saturation

Back 2

–Alveolar levels of 100 mmHg giveshemoglobin saturation

• Alveolar levels of 60 mmHg gives 90%hemoglobin saturation (high altitudes,compromised pulmonary ventilation)

–Tissue levels of 40 mmHg – hemoglobinsaturation is 75%

• active tissue oxygen levels of 20 mmHg –hemoglobin saturation is 35%

Front 3

PO2 curve for O2 bound heme groups and % concentration in blood (line shape)

Back 3

Front 4

Hemoglobin affinity and relation to human development

Back 4

Front 5

In what three ways does activity effect tissues?

Back 5

• Partial pressure of oxygen ‐ PO2

– Levels of PO2 decrease as tissue becomes more active

• pH level

– More acidity in tissues as they become moreactive

• Temperature

– Temperatures increase in active tissues

Front 6

Bohr Effect and root effect

Back 6

– Bohr effect or shift

• Decrease in pH or increase in PCO2 reduces oxygenaffinity; “right shift”

• P50 is increased

• Facilitates oxygen transport to active tissues andfacilitates oxygen binding at the respiratory surfaces

– Root effect• A Bohr effect with a reduction in the oxygen carryingcapacity

Front 7

Bohr Effect (graph)

Back 7

Front 8

In what ways is the affinity of O2 affected

Back 8

• Temperature– Increases in temperature decrease oxygen affinity;“right shift”– P50 is increased

• pH & CO2– Decrease in pH and increase in CO2 decreaseaffinity; “right shift”

• Organic modulators (e.g., DPG)– Increases in these moddulators decrease oxygenaffinity; “right shift”

Front 9

Taxonomic variation of gas transport (diffusion vs blood)

Back 9

– Sponges, cnidarians, echinoderms, and insectscirculate external medium (water or air) pastalmost every body cell and can rely on diffusion– Larger animals use circulatory systems• Transport of gases in blood

Front 10

Respiratory pigments- function and need

Back 10

• Solubility of oxygen in aqueous fluids is low

• Metalloproteins (respiratory pigments)– Proteins containing metal ions which reversiblybind to oxygen and

– Increase oxygen carrying capacity by 50‐fold

– Three major types of respiratory pigments

• Hemoglobins– Chlorocruorins

• Hemocyanins

• Hemerythrins

Front 11

Hemocyanins (taxonomic groups, metal binder, where it is found in the body, color when oxygenated)

Back 11

• Arthropods and molluscs

• Contain copper directly bound to protein (no heme)

• Usually dissolved in the hemolymph

• Appears blue when oxygenated

Front 12

Hemerythrins (taxonomic groups, metal binder, where it is found in the body, color when oxygenated)

Back 12

• Sipunculids, priapulids, brachiopods, some annelids

• Contain iron directly bound to protein (no heme)

• Usually found inside coelomic cells

• Appears violet‐pink when oxygenated

Front 13

Shapes of O2 concentration curves for myoglobin and hemoglobin and why they are shaped that way

Back 13

Front 14

Root effect (graph)

Back 14

Front 15

Relation between P50 O2 and diphosphoglycerate (DPG)

Back 15

Front 16

O2 transport in trout (graph)

-relation of arterial and venous O2 concentration

-warm vs cold acclimatized

Back 16

Front 17

Blood O2 delivery in cephalopods

Back 17

Front 18

Allometric relationship and hemoglobin affinity

Back 18

• Allometry & hemoglobinaffinity

– Smaller species havehemoglobin with loweroxygen affinity

– Favors oxygen unloadingand higher weight‐specificmetabolic rates

Front 19

hypoxia acclimation in water fleas

Back 19

Front 20

Three ways CO2 is transported in Blood

Back 20

– Small amounts of CO2 gas are transported in theplasma• CO2 is more soluble in body fluids than O2

– Some CO2 binds to proteins• For example, carbaminohemoglobin

– Most CO2 is transported as bicarbonate (HCO3–)

CO2 + H2O<-->H2CO3(carbonic acid)<-->HCO3- (bicarbonate) + H+

• Carbonic anhydrase catalyzes the formation of HCO3–

Front 21

Haldane effect

Back 21

• Deoxygenated bloodcan carry more CO2than oxygenated blood

• The formation of carbaminohemoglobin isfavored on deoxygenated hemoglobin

• Deoxygenated hemoglobin is a better protonacceptor than the oxygenated form

-Allows for transport of H+ (proton in hemoglobin), and carbaminohemoglobin

Front 22

creation of HCO3- and release

Back 22

-created by carbonic anhydrase in the red blood cells

-Is then exchanged into the plasma through Cl- ion (to balance charge)

-At respiratory surface transforms back into carbondioxide and water

HCO3- + H+ <--> CO2 +H2O

Front 23

diagram of CO2 transport

Back 23

Front 24

Haldane effect (graphs)

Back 24

Front 25

Relation between PCO2, pH and HCO3-

Back 25

Front 26

blood pH and temperature

Back 26