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Biology
Bio topic 3
haemoglobin
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Cards (57)
What is the function of red blood cells?
To transport
oxygen
in the blood
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What type of structure does hemoglobin have?
Quaternary structure
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How many polypeptide chains does hemoglobin contain?
Four
polypeptide chains
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What is the role of heme groups in hemoglobin?
They bind oxygen due to
iron content
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What is myoglobin's function compared to hemoglobin?
Stores oxygen at low
partial pressures
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What are the key phrases related to the oxyhemoglobin dissociation curve?
Affinity
Saturation
Loading
(Association)
Unloading
(Dissociation)
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What does the term 'affinity' refer to in hemoglobin's function?
Ability to attract or bind
oxygen
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What does 'saturation' mean in the context of hemoglobin?
Maximum amount of
oxygen
bound to hemoglobin
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What is 'loading' or 'association' in hemoglobin function?
Oxygen binding
to hemoglobin
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What does 'unloading' or 'dissociation' refer to?
Oxygen
detaching
from
hemoglobin
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How is the oxyhemoglobin dissociation curve described?
As a
sigmoid curve
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What happens to hemoglobin at high partial pressures of oxygen?
It
becomes
almost
completely
saturated
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What is the saturation level of hemoglobin at low partial pressures of oxygen?
About
50%
saturation
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Why is lower affinity for oxygen at low partial pressures advantageous?
It
unloads
oxygen
where
needed
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What occurs at high partial pressures of oxygen regarding hemoglobin's affinity?
Hemoglobin has a
high
affinity for oxygen
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What is cooperative binding in hemoglobin?
First
oxygen
binding eases subsequent bindings
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What is the Bohr effect?
Effect of
carbon dioxide
on
hemoglobin's
affinity
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What happens to blood pH when carbon dioxide levels are high?
Blood
becomes
more
acidic
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What does a rightward shift in the oxyhemoglobin curve indicate?
Decreased
affinity for oxygen
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What is the significance of a leftward shift in the oxyhemoglobin curve?
Increased
affinity
for oxygen
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How does fetal hemoglobin differ from adult hemoglobin?
Fetal
hemoglobin has a higher affinity for
oxygen
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Why does fetal hemoglobin need a higher affinity for oxygen?
To extract oxygen from
maternal
blood
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Why do llamas have a leftward shifted hemoglobin curve?
To adapt to high
altitudes
with low oxygen
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What advantage does a rightward shifted curve provide for doves?
More readily
unload
oxygen
for
metabolism
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How do earthworms adapt to low oxygen environments?
By having
hemoglobin
with higher
affinity
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What are the key points about hemoglobin's role in oxygen transport?
Hemoglobin is a
quaternary protein
.
It binds oxygen in high
partial pressure
areas.
It unloads oxygen in low partial pressure areas.
Cooperative binding enhances oxygen loading.
The
Bohr effect
influences oxygen unloading.
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How do different types of hemoglobin adapt to their environments?
Fetal
hemoglobin
: Higher affinity for oxygen.
Llama hemoglobin: Higher affinity for low oxygen.
Dove
hemoglobin
: Lower affinity for rapid oxygen unloading.
Earthworm hemoglobin: Higher affinity for underground oxygen.
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What is the structure of haemoglobin?
Quaternary
structure with
4
polypeptide
chains
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How many alpha and beta chains does haemoglobin have?
2
alpha and 2 beta chains
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What does each haem group in haemoglobin contain?
A
ferrous ion
(Fe
2
+
^{2+}
2
+
)
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How many oxygen atoms can haemoglobin carry?
Carrying a total of
8
oxygen atoms
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Why do haemoglobins vary across different organisms?
Due to differences in extreme
environments
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What happens to haemoglobin in low oxygen environments?
It allows oxygen to attach easily
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What is oxyhaemoglobin?
Haemoglobin
combined
with
oxygen
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What is the role of haemoglobin in the body?
Associate with
oxygen
and dissociate to
tissues
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How does haemoglobin change its affinity for oxygen?
It changes in certain
conditions
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What occurs when the first oxygen molecule binds to haemoglobin?
It changes the
protein
shape for more binding
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What is positive cooperativity in haemoglobin?
Binding of one
oxygen
increases binding of others
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What does the oxygen dissociation curve illustrate?
The relationship between
oxygen saturation
and PO
2
_{2}
2
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What happens at higher partial pressure of oxygen?
Increases affinity for oxygen in
haemoglobin
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