Transport In Plants And Animals Flashcards

1
Q

Loading/association def

A

The process by which haemoglobin binds with oxygen (in the lungs)

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2
Q

Unloading/associating

A

The process by which haemoglobin releases its oxygen (in the tissues)

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3
Q

Primary structure of haemoglobin molecules

A

A sequence of amino acid’s in the four polypeptide chains

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4
Q

Secondary structure of haemoglobin molecules

A

Each of the polypeptide chains are coiled into helix

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5
Q

Tertiary structure of haemoglobin molecules

A

Each polypeptide chain is folded into a precise shape which is important for its ability to carry oxygen

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6
Q

Quaternary structure of haemoglobin molecules

A

All four polypeptides are linked together to form an almost spherical molecule. Each polypeptide is associated with the haem group which contains Fe^2+ ions (ferrous). Fe^2+ ions can combine a single oxygen molecule making a total of four molecules carried around by a single haemoglobin molecule

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7
Q

What does decreased affinity for oxygen mean?

A

It’s more difficult for hemoglobin to bind to oxygen (requiring a higher partial pressure of oxygen to achieve the same oxygen saturation), but it makes it easier for the hemoglobin to release oxygen bound to it

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8
Q

What affects haemoglobins affinity for oxygen?

A

Partial pressure. pH. Concentration of CO2 and O2. Temperature

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9
Q

How does haemoglobin officially transport oxygen?

A

It readily associate with oxygen at the surface where gas exchange takes place. It readily dissociates oxygen at those tissues requiring it.

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10
Q

Affinity def

A

Chemical attraction

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11
Q

Where and in what conditions is oxygen associated?

A

Gas exchange surfaces and oxygen concentration is high, carbon dioxide concentration is low and the affinity of haemoglobin for oxygen is high

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12
Q

Where and in what conditions is oxygen dissociated?

A

Respiring tissues with low oxygen concentration, high carbon dioxide concentrations and affinity of haemoglobin for oxygen is low

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13
Q

Oxygen dissociation curve def

A

A graph of the relationship between the saturation of haemoglobin with oxygen in the partial pressure of oxygen

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14
Q

The further left to the curve in an oxygen dissociation curve…

A

The greater the affinity of haemoglobin for oxygen so it loads oxygen readily and unloads less easily

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15
Q

The further right to the curve in an oxygen dissociation curve…

A

The lower the affinity of haemoglobin for oxygen so it loads oxygen less readily but unloads it more easily

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16
Q

Double circulatory system def

A

Blood passes twice to the heart for a complete circuit of the body

17
Q

Closed circulatory system def

A

Blood is confined to vessels in the body

18
Q

Atrium

A

Thin-walled and elastic and it stretches as it collects blood

19
Q

Ventricle

A

Has a thicker muscular wall as it has to contract strongly to pump blood some distance either to the lungs for the rest of the body

20
Q

Bicuspid valve

A

Left atrioventricular (between left atrium and left ventricle) to prevent backflow of blood

21
Q

Tricuspid valve

A

Right atrioventricular (between right atrium and right ventricle) to prevent backflow of blood

22
Q

Diastole

A

Relaxation of the heart

23
Q

Systole

A

Contraction of the heart

24
Q

Semi-lunar valves

A

In the aorta and pulmonary artery to prevent backflow of blood into the ventricles

25
Q

Pocket valves

A

In veins

26
Q

Cardiac ouput

A

Heart rate x stroke volume

27
Q

Heart rate

A

How many beats per minute

28
Q

Stroke volume

A

Volume of blood pumped out per beat

29
Q

Transport of water in plants

A

Transpiration through the xylem

30
Q

Transport of sugars in plants

A

Translocation through the phloem

31
Q

Positive cooperativity

A

When one oxygen joining onto a subunit on a haemoglobin molecule induces other oxygen molecules to bind

32
Q

Why does the oxygen dissociation curve flatten at high partial pressures?

A

There is a low likelihood that the oxygen will bind to the haemoglobin as most of the subunits are already occupied

33
Q

Why does carbon dioxide affect dissociation of oxygen from haemoglobin?

A

Dissolved CO2 is acidic and the low pH changes haemoglobin’s shape