Biochemistry Flashcards

1
Q

what are properties of a mature RBC

A

Packed with haemoglobin (Hb)
No nucleus or mitochondria
No DNA/RNA, therefore no cell division

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2
Q

what is the life span of a RBC

A

120 days

spleen removes old RBC from circulation

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3
Q

what happens to old RBCs

A

recycled by phagocytic cells of the liver and spleen

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4
Q

what is the RBC broken down to

A

Haemoglobin broken down to&raquo_space; amino acids

Haem group (minus iron) is converted to bilirubin

Iron binds to transferrin in the blood and is recycled

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5
Q

where does bilirubin go

A

transported to the liver and secreted into bile

Bilirubin breakdown products colour urine and faeces

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6
Q

what regulates erythrocyte production

A

erythropoietin (EPO) produced by the kidney

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7
Q

what causes the kidney to release EPO

A

hypoxia

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8
Q

what are the steps of erythropoiesis

A

1 - proerythroblast (derived from myeloid stem cells)
2 - polychromatic erythroblast (Hb appears in cytoplasm)
3 - orthochromatic erythroblast (nucleus shrinks, full complement of Hb in cytoplasm)
4 - erythroblast extrudes nucleus
5 - reticulocyte into circulation
6 - mature RBC/erythrocyte

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9
Q

what is the structure of a RBC and why is it important

A

biconcave disc

  • increases SA
  • flexible membrane so cell can squeeze through capillaries
  • decreased diffusion distance
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10
Q

what is the percentage of what blood is composed of

A

55% plasma
1% platelets + WBC

40-50% RBC (in males)
36-46% RBC (in females)

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11
Q

how is a RBC ion balance and cell volume regulated

A

energy-dependent Na+/K+ ATPases (‘the sodium pump’)

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12
Q

through what route does a RBC do ATP synthesis

A

anaerobic glycolysis

no mitochondria so cannot do aerobic glycolysis

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13
Q

what from glycolysis keeps iron in the Fe2+ state

A

NADH

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14
Q

what release oxygen from haemoglobin when we move to a higher altitude

A

2,3 BPG (biphosphoglycerate)

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15
Q

what is Glutathione

A

Tripeptide, consisting of glutamate, cysteine, and glycine

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16
Q

what is the role of Glutathione

A
Reduced glutathione (GSH) combats oxidative stress
i.e. an antioxidant 

maintains normal reduced state in a cell

17
Q

what are free radicals

A

highly reactive molecules with unpaired electrons

18
Q

what would happen if we had excessive free radicals or inadequate antioxidants

A

damage of cellular structures and enzymes

19
Q

what is the importance of glutathione

A

helps protect against the toxic effects of reactive oxygen species (free radicals)

essential to de-toxify hydrogen peroxide

20
Q

what is needed to produce glutathione

A

NADPH from the pentose phosphate pathway

21
Q

how is CO2 carried to the lungs

A

1- Physically dissolved in solution (amount ∝ Pco2)

2 - Bound to Hb – carbamino-haemoglobin

3 - As bicarbonate ion – HCO3-

22
Q

how is the movement of CO2 facilitated

A

by carbonic anhydrase

23
Q

what is haemoglobin comprised of

A

4 globin (protein) sub-units, each containing a single haem molecule

24
Q

what does each haem molecule contain

A

single Fe2+ ion

porphyrin ring

25
Q

what can each haem group bind too

A

one O2 molecule

26
Q

what does haemoglobin synthesis require

A

synthesis of globin chains – 4 per molecule of Hb

synthesis of porphyrin ring (haem group)

insertion of iron (Fe2+) into haem

27
Q

what are normal haemoglobin concentration

A

male = 130-180

female = 115-165

28
Q

how does foetal Hb differ from adult

A

has a higher affinity for O2

has a lower affinity for 2.3 BPG

facilitates the transfer of O2 from the mother to the foetus