Structure and function of normal red blood cells Flashcards

(48 cards)

1
Q

red blood cells have a many ————– to keep the ion concentrations right

A

sodium-potassium pumps

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2
Q

sodium potassium pumps help

A

keep water out

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3
Q

what is the structure of hemoglobin?

A

2 alpha chains and 2 beta chains

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4
Q

hemoglobin is a ——————- protein

A

tetrameric globular

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5
Q

what is the heme group?

A

fe2+ and flat porphyrin ring

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6
Q

how many heme groups are there?

A

one heme per subgroup

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7
Q

one oxygen molecule binds to

A

one Fe2+

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8
Q

what are the functions of haemoglobin?

A

deliver oxygen to tissues
act as a buffer for H+
CO2 transportation

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9
Q

where is the hypoxia sensor located?

A

in the juxtaglomerular apparatus in the kidneys

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10
Q

erythropoietin is produced in the?

A

kidneys

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11
Q

erythropoietin stimulates ———— to undergo hyperplasia?

A

erythron

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12
Q

the erythron is located in the?

A

bone marrow

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13
Q

what are the raw materials required to make red blood cells?

A

iron, folate and B12

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14
Q

what type of response is red cell production?

A

negative feedback

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15
Q

where does red cell destruction normally take place?

A

spleen (and liver)

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16
Q

what is the average life-span of red blood cells

A

120 days

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17
Q

which cells take out aged red cells?

A

macrophages

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18
Q

the globe chains are recycled to?

A

amino acids

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19
Q

what is the heme group broken down to?

A

iron and bilirubin

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20
Q

bilirubin is taken to?

A

liver and conjugated

21
Q

conjugated bilirubin is present in?

A

bile (colors faeces and urine)

22
Q

lots of free radicals are generated from?

A

the oxygen present around the red cell

23
Q

how can freee radicals cause challenges for red cells?

A

they oxidize Fe2+ to Fe3+

damage proteins

24
Q

what is the glycolysis pathway called?

A

embed-meyerhof pathway

25
what is sacrificed to prevent oxidation of Fe2+ to Fe3+
NADH
26
what is Fe3+ called?
metHB
27
what prevents oxygen from becoming superoxide?
superoxidase dismutase
28
what does superoxide cause?
interacts with proteins, DNA etc and damages their structure
29
what converts hydrogen peroxide to water?
peroxidase catalase
30
superoxide is converted to?
hydrogen peroxide
31
what protects us from hydrogen peroxide by reacting with it to form water?
glutathione
32
when glutathione reacts with hydrogen peroxide you get?
water and an oxidized glutathione product
33
how is oxidized glutathione replenished?
NADPH
34
what generates NADPH?
the hexose monophosphate shunt
35
what is the rate-limiting enzyme in this process?
glucose-6-phosphate dehydrogenase
36
majority of CO2 is transported as?
bicarbonate
37
in tissues Co2 and water make?
H2CO3
38
what enzymecatalyses Co2 and Water?
Carbonic anhydrase
39
H2CO3 then forms?
H+ and HCO3- and Cl-
40
where does Cl- come from?
it enters to presence potential
41
how is H= buffered?
by deoxygenated Hb
42
how is HCO3- exported?
facilitated diffusion between Cl-
43
what is the Hb allosteric effect?
as one oxygen bind to a subunit the Hb changes shape and this alters how easy it is for the next O2 to bind to a different subunit changing shape again, cooperative binding
44
what is different about foetal hemoglobin?
as maternal blood flows through the placenta at the same partial pressure, there is increased foetal hemoglobin saturation than normal haemoglobin saturation
45
small molecules can interact with Hb and?
affect the shape of the curve and how much oxygen is delivered to the tissues
46
in chronic anaemia what pathway is activated?
Rapapoport-Lubering shunt
47
this is when 1,3 bisphosphoglycaerate is converted to?
2,3,BPG
48
2,3, BPG causes the curve to shift?
to the right resulting in more O2 delivered to tissues