red blood cell structure and function Flashcards

1
Q

how many polypeptide chains does heamoglobin contain

A

4

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2
Q

what are the 4 polypeptide chains

A

2 alpha globin chains

2 beta globin chains

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3
Q

where does ferrous iron come from

A

circulating transferring and protoporphyrin

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4
Q

what is the synthesis of red blood cells called

A

erythropeoisis

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5
Q

what does carbon dioxide combine with and what does this create

A

water to produce carbonic acid

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6
Q

what enzyme produces carbonic acid

A

carbonic anhydrase

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7
Q

what is the chloride shift

A

carbonic acid breaks down into H+ and HCO3-

HCO3- moves out in exchange with Cl-

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8
Q

what is most CO2 transported as

A

bicarbonate

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9
Q

how is haemoglobin produced

A

Glycine and succinyl coA react to produce protoporphyrin - this is synthesised by ALA-synthase pyroxidine

protoporphyrin then combines with Fe+ to form the haem group

this then combines with globin to produce heamoglobin

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10
Q

what is the first recognisable RBC precursor in the bone marrow

A

proerothroblast

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11
Q

what does the proerothroblast undergo maturation into in the marrow

A

late normoblast

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12
Q

what happens to form a reticulocyte

A

the nucleus is extruded when pushed into the blood - this contains some residual ribosomal RNA and so can still synthesise some haemoglobin (however after a couple of days in the blood the RNA degrades and the mature RBC cannot synthesise any more heamoglobin)

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13
Q

what stimulates erythropoiesis

A

erythropoietin

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14
Q

what is erythropoietin

A

a glycosylated peptide mostly produced in the kidney

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15
Q

when is there major production of erythropoietin

A

when theres low oxygen tensions

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16
Q

how does lower oxygen tensions cause the release of erythropoeiten

A

because RBCs give oxygen to the kidneys which have oxygen sensors
if oxygen levels are low then this causes the peritubular interstitial cells of the outer cortex to release more erythropoietin

17
Q

when does erythropoietin act on

A

the later stages of RBC maturation when it still has a nucleus

18
Q

what is special about the RBC membrane

A

lipid bilayer

19
Q

what does the inside of the lipid bilayer contain

A
spectrin
ankyrin 
actin 
protein 4.1
band 3 proteins (anion channels) 
carbohydrate chains
20
Q

how do RBC derive their energy

A

from glycolytic pathways

21
Q

what controls the oxygen-deoxygynation of haemoglobin

A

2,3, DPG

when haemoglobin is oxygenated there is no space for 2,3 DPG to fit in

when deoxygenated 2,3 DPG can fit in the middle and allow rapid release of O2

22
Q

where is prenatal heamoglobin synthesised

A

in the yolk sac, then the liver and then the spleen.

23
Q

RBC’s under normal circumstances are broken down how

A

extravascularly in macrophages

24
Q

what is protoporphyrine converted into

A

bilirubin

25
Q

how does RBC lysis occur abnormally

A

intra-vascular

26
Q

where are the hydrophilic AA’s postitioned

A

project outwards making RBC soluble

27
Q

where are the hydrophobic AA’s positioned

A

project inwards making interior of Hb water repellant

28
Q

what is protoporphyrine anchored by

A

F8 histadine

29
Q

what are the chemical bonds that hold the quaternary structure of haemoglobin together

A

ionic, hydrogen and van der waals