hameproteins 2 Flashcards

1
Q

left shift has : — affinity for 02
right shift has: — of o2 due to the – of ph and – of h+ concentration. The h+ and 02 both compete for the binding to —

A
  • high
  • low
  • decrease ph
  • increased H
  • hemaoglobin
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2
Q

if we — the acidity and — h+ the haemoglobin will becomes less likely to bind to 02 for a given po2

A
  • increased , increased
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3
Q

at 40mmhg of 02 — % ~ to haemoglobin at ph — saturated
at 40mmgh > of 02 > – of haemoglobin at ph – saturated w/ o2

A
  • 45% , 6.8
  • 80% , 7.6
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4
Q

oxygenation occurs in the

A

lungs

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5
Q

at the lungs 02 levels are —

A

high

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6
Q

02 levels in the muscles are — and ph is — due to —-

A
  • low
  • low
    -respiration
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7
Q

the affinity of myoglobin for o2 is — than haemoglobin and 02 will be transferred from – to —-

A
  • higher
  • oxyhemoglobin
    -myoglobin
  • fromula: hb+ (02)4 equilibrum hb+ 4 02 equilibrum 4 Mb02
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8
Q

at the muscles — occurs by using — to produce — hence muscle’s ph is — and 02 levels are —

A
  • respiration
  • 02
    -co2
    low
  • low
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9
Q

H+ is produced in the — by —–

A

muscles , metabolism

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10
Q

haemoglobin also transports — and — . Free — at the muscles will bind to — and — and transports it to the —

A
  • co2 and h+
  • heamoglobin
  • c02 and h+
  • lungs
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11
Q

most co2 produced in — reacts with — by the catalyst — and is converted into —- in erythrocytes

A
  • respiration
  • water
  • carbonic anhydrase
  • bicarbonate ( HCO3-)
  • formula: co2 + h20 —> <— hco3- + h+
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12
Q

some co2 will react with haemoglobin to form — which is — and —

A
  • haemoglobin
  • carbomate
  • carboxylic acid with an animo group
  • fromula: c02 + R-NH2 equilibrum crabomate + h+
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13
Q

h+ are transported by – to the side chains of the number of amino acids risidues and produces — charged groups

A
  • binding
  • positive
  • ( the amino acid residues in proteins are numbered, so histadine 122 alpha is 122nd amino acid residue from the end of the alpha chain )
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14
Q

— is a compact tense structure which the globin chains interact with —- so haemoglobin is said to be in a — state

A
  • haemoglobin
  • salt linkages/ electrostatic
  • t- state ( tense , taut )
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15
Q

the process of cooperative oxygen binding aka cooperativity :

A
  • addition of the first 02 to haemoglobin is difficult
  • when this happens the fe II will be converted from high spin to low spin
  • this causes the fe II to shrink and moves into the porphyrin plane
  • proximal histadine attached to iron moves w/ it
  • globin chain which histadine belongs to also moves
  • causes breakage in the salt bridges and the whole structure will relax and opens
  • the other heam group becomes exposed and 2nd,3d,4th 02 molecule can be added
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16
Q

the protein in the oxyhemoglobin is in the — sate since there are few — present in the haemoglobin

A
  • R-state , relaxed
  • few salt linkages
17
Q

— protein is one which interaction at one site in the molicule affects interaction of the remote site

A
  • allosteric protein
18
Q

which of those are allosteric protein: - haemoglobin
- myoglobin
- both
- none

A
  • haemoglobin
19
Q

allosteric effects in haemoglobin includes:

A
  • 02 binding in one site will help the 02 binds in the remote site in the same molecule
  • binding of h+ and c02 in a site results in charged groups being formed which promotes the formation of salt bridges ( ie. t state ) which squeeze the 02 out
  • binding of 02 to haemoglobin in alveolar capillaries of the the lungs causes the breaking of salt bridges and releasing of c02 and h+
20
Q

the inter relationship between h+ , co2, and 02 is known to be:

A

bohrs effect

21
Q

— is produced when c is burned in the presence of 02 and the properties are —

A

carbon monoxide
- 2c + 02 –> 2co
- colorless , ouderwets cab ve found in the vehicles of the exhaust fumes , house fires or poorly maintained oil and gas hearers. also known as the: silent killer

22
Q

why is CO toxic?

A
  • the affinity of haemoglobin to co is 225 times greater than its affinity for 02
  • binding is string and is irrversable
  • affinity of myoglobin for co is 25 times greater than 02
23
Q

hb + 4 co –> hb ( co) 4 is known as

A

carbomoxoheamomyglobin

24
Q

If the fe-c trible bond 0 was – no — would be involved in the affinity for haemoglobin for c trible bond 0 and it would be —- times greater than affinity for — which means any exposure would kill us

A
  • linear
  • no hydrogen bonding
  • 25,000 greater
  • 02
25
Q

affinity of haemoglobin for co is only — than 02 because of the —- of stability of the co complex increases the stability for —

A
  • 225
  • reduction of stability
  • 02
26
Q

— is located close to 02 and co binding site forces the co to bind in an — which — the complex which is considered to be a —-

A
  • distal histadine ( no fe coordinated unlike proximal )
  • angle
  • destabilises
  • steric effect
27
Q

02 is stabilised by the presence of —- between partially — on non bridging oxygen and the distal histadine

A

-strong h+
- negative

28
Q

—- stabilises the oxyhemaoglobin by — more than it does in —-
which is the most important thing.

A
  • distal histadine
  • hydrogen bonding
  • carbinmonxohymoglobin
29
Q

AGAIN LOL: why is it toxic:
- hydrogen bonding between – and — stabilises the — of haemoglobin much more than —

A
  • 02
  • distal histadinbe
  • 02 complex
  • ( the poison is treated by administering 02 under high pressure 2 or 3 atm as in hyperbaric )