OXYGEN DISSOCIATION CURVE

Question 1

HAEMOGLOBIN

Answer 1

haemoglobin is a protein with a quarternery structure.

Question 2

affinity of haemoglobin

Answer 2

ability of haemoglobin tp attract or bind oxygen.

Question 3

saturation of haemoglobin

Answer 3

the maximum oxygen a haemoglobin can bind to

Question 4

loading or association

Answer 4

when oxygen is binding to haemoglobin.

Question 5

unloading or dissociation.

Answer 5

when oxygen detatches from the haemoglobin.

Question 6

oxyhaemoglobin dissociation curve

Answer 6

oxygen is loaded in a high partial pressure of oxygen ( alveoli) and oxygen is unloaded in a region where there is low partial pressure.( respiring tissues). this is called the oxyhaemoglobin dissociation curve. it is sigmoid in shape.

Question 7

co operative bonding

Answer 7

the co operative nature of oxygen is due to the change in shape of the haemoglobin when the first oxygen binds with it. this makes it easier for further oxygen molecules to bind.

Question 8

bohr effect

Answer 8

bohr effect is when there is a high concentration of carbon dioxide which shifts the oxyhaemoglobin curve to the righ decreasing the oxygen affinity because a high number of co2 is produced and changes the shape of the haemoglobin slightly.

Question 9

advantage of bohr shift

Answer 9

when exercising, co2 is released in alarge amount. which decreases the saturity of the haemoglobiin so more oxygen is released to the respiring tissues and more energy is released.

Question 10

foetal haemoglobin

Answer 10

shifts to left - has higher affinity than adult haemoglobin because it allows them to steal oxygen from mothers hae oglobin.