Lecture 7 and 8: Haemoglobin, Protein Structure and Gas Transport Flashcards

1
Q

List the levels of protein structure.

A

Primary
Secondary
Tertiary
Quaternary

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2
Q

What is deoxyhaemoglobin?

A

Tense (T) state.
Hb
Reduced haemoglobin

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3
Q

What is oxyhaemoglobin?

A

Haemoglobin that is bound with O2.
Relaxed (R) state
Hb(O2)4

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4
Q

List the structural features that make haemoglobin well suited to transporting O2 and CO2.

A
  • Can vary its affinity for binding O2

- Cooperative binding

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5
Q

How is O2 transported in the blood?

A
  1. 5% dissolved in the plasma

98. 5% bound to haem groups of Hb in RBCs

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6
Q

How is CO2 transported in the blood?

A

As HCO3- (bicarbonate) (70%)
Carbamino compounds combined with proteins (20 - 23%)
Dissolved in plasma (7 - 10%)

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7
Q

What is cyanosis?

A

A decrease in blood saturation O2 levels. Poisoning can cause.

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8
Q

What is the Bohr effect?

A

Haemoglobin’s affinity for O2 decreases in the presence of low pH (acidic) or high CO2 conditions. This causes an increase O2 delivery to tissues with those conditions.

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9
Q

Decreasing pH will __________ haemoglobin’s affinity for O2.

a. decrease
b. increase
c. have no effect on

A

a. decrease

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10
Q

What is the Haldane effect?

A

The CO2 content of deoxgenated blood is greater than oxygenated blood.
Therefore, when blood releases O2 (becomes deoxygenated), it can take up more CO2.

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11
Q

Decreasing CO2 concentrations will __________ haemoglobin’s affinity for O2.

a. decrease
b. increase
c. have no effect on

A

b. increase

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12
Q

What is the Bohr effect?

A

Haemoglobin’s affinity for O2 decreases in the presence of low pH (acidic) or high CO2 conditions. This causes an increase O2 delivery to tissues with those conditions.
Facilitates O2 delivery to tissue.

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13
Q

Decreasing pH will __________ haemoglobin’s affinity for O2.

a. decrease
b. increase
c. have no effect on

A

a. decrease

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14
Q

What is the Haldane effect?

A

The CO2 content of deoxgenated blood is greater than oxygenated blood.
Therefore, when blood releases O2 (becomes deoxygenated), it can take up more CO2.
Facilitates CO2 delivery to lungs.

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15
Q

Increasing temperature will __________ haemoglobin’s affinity for O2.

a. decrease
b. increase
c. have no effect on

A

a. decrease

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16
Q

Binding 2, 3-DPG to deoxyhaemoglobin will __________ its affinity for O2.

a. decrease
b. increase
c. have no effect on

A

a. decrease

17
Q

List the factors that regulate the rate hemoglobin binds and releases O2.

A

Partial pressure of O2 and CO2
pH
Temperature
Concentration of BPG

18
Q

What is saturated haemoglobin?

A

Saturated haemoglobin has O2 bound to all four haem portions.

19
Q

What is partially saturated haemoglobin?

A

Partially saturated haemoglobin has O2 bound to one to three haem portions.

20
Q

What percentage of bound O2 is unloaded during one circuit of systemic circulation?

A

25%