haemoglobin Flashcards

1
Q

definition of saturation

A

amount of oxygen combined with haemoglobin

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2
Q

structure of haemoglobin

A

complex protein, quaternary structure (4 poplypeptide subunit - each containing a haem group), globular

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3
Q

uptake of oxygen by haemoglobin reaction
(word and symbol equation)

A

Hb+ 4O2 >< Hb(O2)4

haemoglobin + oxygen >< oxyhaemoglobin

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4
Q

percentage saturation of Hb calculation

A

percentage saturation of HB with O=

oxygenated Hb/ max saturation X100

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5
Q

why is the oxygen dissociation curve a sigmoid shape

A

binding of the first oxygen changes the tertiary structure of haemoglobin
uncovering another haem group/ binding site for the 2nd and 3rd oxygen to bind to

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6
Q

what happens to the oxygen dissociation curve with a small animal

A

shifts right
have high Sa: Vol ratio so more heat is lost
a higher metabolism is needed to maintain their body temp
lower affinity at higher pO2 - more oxygen unloaded at tissues for aerobic respiration

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7
Q

what happens to the oxygen dissociation curve at areas with low pO2
(underground, high altitude)

A

shifts left
more O2 loaded at low pO2
transported to tissues for aerobic respiration
higher affinity at lower pO2

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8
Q

what happens to the oxygen dissociation curve at high levels of CO2

A

shifts right
CO2 lowers pH of blood causing Hb tertiary structure changes
lower affinity at higher pO2
Bohr shift to the right

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