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Haematology > Normal RBCs > Flashcards

Normal RBCs Flashcards

1
Q

What component of RBC carries O2

A

Hb

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2
Q

RBC do/not have a nucleus

A

do not

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3
Q

RBCs do/not have mitochondria

A

do not

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4
Q

What does a high SA:V ratio allow for in the RBC

A

gas exchange

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5
Q

What is a consequence of RBC being packed with Hb

A

creates a high oncotic pressure - cell wants to swell

O2 rich environment - risk of oxidation and damage

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6
Q

consequence of no mitochondria in RBC

A

energy production limited to glycolysis

- low energy yield

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7
Q

what is special about the RBC membrane

A

it is complex

contains proteins which make it flexible

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8
Q

How is water kept out of RBCs

A

via Na/K ATPase

this requires energy

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9
Q

Describe the structure of Hb

A

tetrameric globular protein
2 alpha and 2 beta chains - globin
haem = Fe2+ and porphyrin ring

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10
Q

O2 can bind to Fe3+, true or false

A

FALSE

O2 can only bind to Fe2+

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11
Q

What are the chemical symbols for ferrous and ferric

A 
ferrous = Fe2+
ferric = Fe3+
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12
Q

what is the function of Hb

A

carry oxygen to tissues
acts as a buffer for H+
involved in CO2 transport

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13
Q

which hormone regulates RBC production and from where is it secreted

A

erythropoeitin

kidneys

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14
Q

where and what happens in RBC destruction

A

occurs in spleen
macrophages take up aged cells
raw materials are recycled

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15
Q

what is the pathway in the breakdown of haem

A 
haem 
biliverdin 
unconjugated bilirubin 
conjugated bilirubin 
urobilinogen - urine
stercobilinogen - stool
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16
Q

what can the presence of free radicals cause

A

oxidation of Fe2+ to Fe3+ meaning it cant carry O2

causes damage to proteins

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17
Q

what is the Embden-Meyerhof pathway also known as

A

Glycolysis

ATP production in the absence of O2

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18
Q

what is the overall net gain in glycolysis

A

2 ATP + NADH

19
Q

what molecule is used to prevent oxidation of Fe2+ to Fe3+

A

NADH (proton donor)

20
Q

What are reactive oxygen species

give examples

A

free radicals containing unpaired electrons - damaging

superoxide and hydrogen peroxide (H2O2)

21
Q

which enzyme converts superoxide into H2O2

A

superoxide dismutase

22
Q

what does catalase do

A

convert H2O2 into H20

23
Q

what is the function of Glutathione (GSH)

A

protects us from H2O2by binding with it to form H20 and an oxidised side product GSSG

24
Q

How does GSSG become GSH again

A

via NADPH

25
Q

How is NADPH generated

A

via hexose monophosphate shunt

26
Q

which enzyme is the rate limiting enzyme in the hexose monophosphate shunt

A

G6PD

27
Q

How is CO2 transported to the lungs

A

10% dissolved in solution
30% bound to Hb
60% as bicarbonate

28
Q

Cl- entry into RBC causes it to swell/shrink

A

swell

29
Q

Cl- exit from RBC causes it to swell/shrink

A

shrink

30
Q

what is partial pressure of a gas

A

pressure that a gas (in a mixture of gases) would exert if it were alone

31
Q

how many O2 molecules bind to Fe2+ in haem

A

1

32
Q

how many O2 molecules bind in 1 RBC

A

4

33
Q

at the lungs, pO2 is high/low

A

high

Hb needs to bind easily

34
Q

at the tissues, pO2 is high/low

A

low

Hb needs to release O2

35
Q

What pattern is shown when O2 binds to haem

A

allosteric effect

36
Q

what is cooperative binding

A

binding of 1 O2 molecule makes it easier to bind the next etc…

37
Q

For the same pO2, you will saturate more HbF than HbA, true or false

A

true

38
Q

what is the shape of the curve in HbA binding

A

sigmoid curve

39
Q

in which pathway is 2,3 BPG generated

A

Rapapoport-Lubering Shunt

40
Q

what activates the Rapapoport-Lubering Shunt

A

chronic hypoxia and anaemia

increase 2,3 BPG levels

41
Q 
high levels of:
H+
2,3BPG
temperature 
causes a shift to the left/right?
A

right

42
Q 
low levels of:
H+
2,3BPG
temperature 
causes a shift to the left/right?
A

left

43
Q

more oxygen is delivered to tissues in times of stress for example

A

anaemia, metabolic acidosis, increased CO2 concentration

Haematology (26 decks)

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