Haemoglobin Flashcards
How is the red blood cell adapted?
bi-concave shape ( increases SA: VOL and short diff. pathway)
contains only haemoglobin ( which increases O2 capacity)
flexible (can bend through narrow capillaries)
Describe the four structures of a red blood cell
primary= sequence of amino acids in the four polypeptide chains
secondary=each chain coiled into a helix
tertiary= filed into precise shape essential for its function
quarternary= all polypeptides link to form an almost spherical molecules, each polypeptide is associated with a beam group ( Fe2+)
How many o2 molecules per HB molecule?
4
Where does Loading/associating occur?
in the lungs
Where does unloading/dissociating occur?
in the tissue
What does ‘high affinity’ mean?
it can uptake o2 easily but releases it less easily
What is the role of HB?
to transport oxygen
How does the HB molecules adapted to different oxygen partial pressures?
it can change its affinity
by changing its 3 in the presence of substances eg. co2
in co2 it binds to the o2 more loosely so o2 can be released
Why are there different haemoglobins?
different amino acid sequence
different oxygen-binding properties
What is an erythrocyte?
red blood cell
The oxygen dissociation curve for haemoglobin shifts to the right during vigorous exercise.
Explain the advantage of this shift.
Lower affinity for oxygen / releases more oxygen / unloads more readily;
(To) muscles / tissues / cells
(For) high / rapid respiration