Haemoglobin Flashcards

1
Q

Why can’t large organisms use diffusion for gas exchange?

A

-they have a small SA:V
-simple diffusion is not sufficient enough to meet the organisms Oxygen demands
-alternative method required to transport oxygen to tissues

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2
Q

How do organisms solve the problem of not being able to have oxygen diffusion into their bodies?

A

-they circulate blood around their bodies to carry oxygen to respiring tissues

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3
Q

Why can’t oxygen just dissolve into the blood?

A

Oxygen has a low solubility in aqueous solutions (such as water)

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4
Q

Structure of haemoglobin:

A

-complex protein quaternary structure
-composed of four polypeptides
-each containing a prosthetic haem group (Fe2+ containing group)

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5
Q

Haemoglobin has an ______ to oxygen

A

Affinity

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6
Q

What is affinity?

A

Chemical attraction

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7
Q

How many oxygen molecules can one haemoglobin molecule combine with?

A

4

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8
Q

How much molecules of haemoglobin are in one red blood cell?

A

300 million

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9
Q

How is haemoglobin efficeint at transporting oxygen?

A

-readily associates at the lungs
-and dissociates at respiring tissues

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10
Q

The uptake of oxygen by haemoglobin is a _____ reaction

A

Reversible

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11
Q

What does oxygen and haemoglobin combining form..?

A

Oxyhaemoglobin

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12
Q

The amount of oxygen combined is described in terms of…

A

percentage saturation of the haemoglobin

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13
Q

formula for calculating the percentage saturation of haemoglobin with oxygen

A

Percentage saturation =

oxygenated haemoglobin
————————————- x100%
maximum saturation

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14
Q

partial pressure of oxygen

A

The proportion of oxygen in a mixture of gases or solution

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15
Q

What happens when ocyhaemoglobin moves to an area of low oxygen concentration?

A

Oxygen is unloaded to the surroundings

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16
Q

An oxygen dissociation curve is what shape?

A

S shaped and described as a sigmoid curve

17
Q

How does the binding of one oxygen molecule make it easier for other oxygen molecules to bind to haemoglobin?

A

-the binding of the first oxygen molecule alters the tertiary structure of the haemoglobin molecule
-this exposes the second and third binding sites
-which makes it easier for the second and third oxygen molecules to bind and load
» referred to as the cooperative nature of oxygen loading

18
Q

Haemoglobin has a higher affinity for oxygen at..

A

a high partial pressure of oxygen

19
Q

The partial pressure of oxygen is h