Mass transport

Question 1

haemoglobin made up of how many polypeptide chains

Answer 1

4 polypeptides

Question 2

what gives haemoglobin its red colour

Answer 2

iron ions

Question 3

loading

Answer 3

haemoglobin binding with oxygen

Question 4

unloading

Answer 4

haemoglobin releasing oxygen

Question 5

when and where is oxyhaemoglobin formed

Answer 5

when O2 is loaded onto haemoglobin it forms oxyhaemoglobin where theres a high pO2

Question 6

where does oxyhaemoglobin unload

Answer 6

where theres a low pO2

Question 7

in the alveoli why does o2 load onto haemoglobin to form oxyhaemoglobin

Answer 7

because o2 enters blood capillaries at alveoli in lungs and the alveoli has a high pO2

Question 8

what do cells use when respiring and what does it do

Answer 8

cells use O2 when respiring and it causes the pO2 to lower which is why red blood cells deliver oxyhaemoglobin to respiring tissues causing it to unload O2 (release)

Question 9

why red blood cells deliver oxyhaemoglobin to respiring tissues

Answer 9

cells use O2 when respiring and it causes the pO2 to lower. red blood cells cause it to unload O2 (release)

Question 10

where is there a high affinity for O2

Answer 10

at the lungs

Question 11

reversible reaction for haemoglobin

Answer 11

Hb+4O2<=>HbO8

Question 12

how does CO2 affect O2 unloading

Answer 12

Hb. gives O2 up easily at high pCO2

Question 13

what do cells produce

Answer 13

CO2 so that raises the pCO2 increasing rate of oxygen unloading

Question 14

if theres a high affinity of pCO2 what affect does that have on the dissociation curve

Answer 14

shifts it to the right

Question 15

role of Hb

Answer 15

transport oxygen

Question 16

how must haemoglobin be efficient when transporting oxygen

Answer 16

1. readily associate with oxygen at the surface where gas exchange takes place
2. readily dissociate from oxygen at those tissues requiring it

Question 17

why do different haemoglobin have different affinities for oxygen

Answer 17

each species produces a haemoglobin with a slightly different amino acid sequence. the haemoglobin of each species therefore has a slightly different tertiary structure and different oxygen binding properties.

Question 18

what is happened at the gas exchange surface

Answer 18

co2 constantly being removed. the ph is raised due to the low conc of co2. that causes the shape of Hb to change into one that can load oxygen more readily

Question 19

in tissues co2 is produced by respiring cells. co2 is acidic in solution so what does that do to the ph of blood

Answer 19

its lowered in tissues. that changes the shape of hb into one with a lower affinity for oxygen. hb releases its o2 into respiring tissues

Question 20

the more active a tissue is the more ___ is ____

Answer 20

the more oxygen is unloaded

Question 21

the higher the rate of respiration -

Answer 21

the more carbon dioxide the tissue produces so the greater the haemoglobin shape change so its more easily oxygen is unloaded so the more oxygen is available for respiration