Mass Transport Flashcards

1
Q

Structure of haemoglobin

A

Globular,water soluble. Consists of a polypeptide chains , each carrying a haem group (quaternary structure)

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2
Q

Role of haemoglobin

A

Present in red blood cells. O2 binds to the haem groups and are carried around the body to where they are needed in respiring tissues.

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3
Q

3 types of haemoglobin

A

Myoglobin
Adult haemoglobin
Fetal haemogobin

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4
Q
A
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5
Q

3 factors affecting oxygen-haemoglobin binding

A
  1. Partial pressure/concentration of O2
  2. Partial pressure/concentration of CO2
  3. Saturation of haemoglobin with oxygen
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6
Q

How does partial pressure of oxygen affect oxygen-haemoglobin binding?

A

As partial pressure of O2 also increases, so oxygen binds tightly to haemoglobin.

When partial pressure is low oxygen is released from haemoglobin

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7
Q

How does partial pressure of oxygen affect oxygen-haemoglobin binding?

A

As partial pressure of oxygen increases, the affinity of haemoglobin for oxygen also increases, so oxygen binds tightly to haemoglobin.

When partial pressure is low oxygen is released from haemoglobin

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8
Q

How does partial pressure of carbon dioxide affect oxygen-haemoglobin binding?

A

As partial pressure of carbon dioxide increases, the conditions become acidic causing haemoglobin to change shape.

The affinity of haemoglobin for O2 therefore decreases , so oxygen is released from haemoglobin. This is known as the Bohr effect.

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9
Q

How does saturation of haemoglobin with oxygen affect oxygen-haemoglobin binding?

A

It is hard for the first oxygen molecule to bind.

Once it does, it changes the shape to make it easier for the second and third molecules to bind, known as positive cooperativity.

It is then slightly harder for the fourth oxygen molecule to bind because there is a low chance of finding a binding site

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10
Q

Explain why o2 binds to haemoglobin in the lungs

A
  1. Partial pressure of O2 is high
  2. Low concentration of CO2 in the lungs, so affinity is high
  3. Positive cooperativity (bidnign becomes easier after the first O2 binds)
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11
Q

Explain why O2 is released from haemoglobin in respiring tissues

A
  1. Partial pressure of O2 is low
  2. High conc. of CO2 in respiring tissues, so affinity decreases.
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12
Q

What does it mean if the oxyhaemoglobin curve shifts to the right

A

High partial pressure of CO2 at respiring tissues

Decrease of affinity and there unloads more O2

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13
Q

What does it mean if the oxyhaemoglobin curve shifts to the left

A

Low partial pressure of CO2 in the alveoli

Increase in affinity and therefore uploads more O2

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14
Q

Why do animals have different types of haemoglobins

A

Different types of haemoglobins have different affinities for O2 which is an adaptation to their environment.

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15
Q

What is tissue fluid?

A

Fluid containing water, glucose , amino acids and fatty acids which bathes the tissue

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16
Q

How is tissue formed?

A

As blood enters the capillaries from the ARTERIOLES, the smaller diameter results in a HIGH HYDROSTATIC PRESSURE, so water, glucose, amino acids, fatty acids, ions, and oxygen are forced out. This is known as ultrafiltration.

17
Q

What remains in the capillary after tissue fluid is pushed out

A

Red blood cells
Platelets
Large proteins

18
Q

How is tissue fluid reabsorbed ?

A

Large molecules that remain in the capillaries and lower water potential. Towards the venule end of the capillaries, the hydrostatic pressure is lowered due to the loss of liquid. So water re-enter the capillaries by osmosis

19
Q
A