Transporting oxygen and carbon dioxide

Question 1

What is the structure of haemoglobin

Answer 1

Large globular protein made up of 4 peptide chains each with an iron containing prosthetic group

Question 2

How does oxyhameoglobin form

Answer 2

molecule formed when oxygen binds to haemoglobin

Question 3

What is the equation to from oxyhaemglobin

Answer 3

Hb + 402 =Hb4O2

Question 4

What happens when the first oxygen molecule that binds to the haemoglobin (disscoation curve)

Answer 4

It alters the arrangement of the molecule making it easier for the following oxygen molecules to bind

Question 5

What is the structure of haemoglobin

Answer 5

Quaternary structure

Question 6

What does this mean “affinity of hameglobin for oxygen”

Answer 6

The ability of haemglobin to attract, or bind oxygen

Question 7

What does this mean

“Saturation of hameglobin with oxygen”

Answer 7

When hameglboin is holding the maximum amount of oxygen it can bind

Question 8

What is “loading/ association of hameglobin”

Answer 8

The binding of oxygen to haemglobin

Question 9

What does this mean “Unloading/ dissociation of haemoglobin”

Answer 9

When oxygen detaches, or unbinds from haemoglobin

Question 10

What happens when we have lower partial pressure of oxygen

Answer 10

`Haemoglobin does not have a high affinity this causes the Haemoglobin to unload oxygen in those regions

Question 11

Why is it an advantage that haemoglobin is unloading at low partial pressure

Answer 11

It means the haemoglobin is unloading oxygen at site where the oxygen is needed

Question 12

What happens when theris lots partial pressure

Answer 12

It has a high affinity for oxygen so it will be loading or associating lots of oxygen

Question 13

What is the Bohr effect

Answer 13

Changes in the oxygen dissociation curve of haemoglobin that occur due to a rise in carbon dioxide levels and a reduction of affinity of haemoglobin for oxygen

Question 14

What happens when the bhor effect takes place

Answer 14

as the proportion of CO2 rises, the hameglobin curve moves down and to the right

Question 15

If the curve shifts left what does that tell us

Answer 15

increased affinity and therefore uploads more oxygen

Question 16

if the curve shifts right what does that tell us

Answer 16

decreased affinity and there for unloads more oxygen

Question 17

How is fetal haemoglobin different to adult haemoglobin

Answer 17

Higher affinity for oxygen even at that same partial pressure of oxygen

Question 18

What is myoglobin

Answer 18

respiratory pigment found in the muscle tissue of vertebrates with a higher affinity for oxygen than haemoglobin

Question 19

What are some similarities between haemoglobin and myoglobin

Answer 19

Both are oxygen carrying pigments composed of heme proteins and iron.

Both proteins are capable of increasing the amount of dissolved oxygen in biological fluids of vertebrates as well as in some invertebrates.

Question 20

What are differences between structure in haemoglobin and myglobin

Answer 20

Quaternary structure in hameglobin

and a monomer and lacks Quaternary structure in myoglobin

Question 21

Diffrences in polypeptide chains in hameglobin and myoglonin

Answer 21

Hemoglboin has 4 PP chains

Myoglobin has single PP chain

Question 22

Oxygen binding ability between hameoglobin and myglobin

Answer 22

Hemoglboin has a low affinity to bind with oxygen

Myoglobin has a high afiinity to bind with oxygen which does not depend on the oxygen concentration

Question 23

How does mylgobin act as storage molecule

Answer 23

when oxygen binds to myglobin it does not give it up very easily

Question 24

When does myoglobin release oxygen

Answer 24

when the oxygen levels in very active muscle tissue get really low the CO2 levels are high myoglobin release its store of oxygen

Question 25

What causes the Bhor affect

Answer 25

presence of co2 is caused by the acidic nature of dissolved co2