Hemoglobin Flashcards

hemoglobin oxygen-hemoglobin dissociation curve

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1
Q

Each alveolus is surrounded by a network of capillaries. What kind of blood does the pulmonary arteries bring to the capillaries?

(carries blood away from the heart)

A

Deoxygenated blood

  • high levels of CO2
  • low levels of O2
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2
Q

Each alveolus is surrounded by a network of capillaries. What kind of blood does the pulmonary veins bring to the capillaries?

(carries blood toward the heart)

A

Oxygenated blood

  • high levels of O2
  • NO levels of CO2
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3
Q

In the respiratory system, is ATP required for gas transfer (O2 and CO2) between the alveoli and blood?

A

NO, because both gases are moving down their concentration gradients.

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4
Q

How is oxygen transported by the blood?

A

Binds to the protein hemoglobin (Hb).

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5
Q

What is hemoglobin?

A

A protein that carries oxygen in the blood.

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6
Q

What gives blood its characteristic red color?

A

Heme groups

(They are prosthetic groups and without heme groups, hemoglobin is inactive.)

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7
Q

When does an enzyme or protein exhibit cooperativity?

A

When there are multiple binding sites or subunits.

One subunit can undergo a conformational change, which either enhances or reduces the activity of the other subunits.

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8
Q

Is hemoglobin (Hb) affected by positive or negative cooperativity?

A

Positive cooperativity

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9
Q

Why is there a sigmoidal shape for an oxyhemoglobin dissociation curve?

A

Because hemoglobin exhibits positive cooperativity.

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10
Q

Explain positive cooperativity in hemoglobin.

*Think of the party example*

A

One O2 molecule binds to a heme group and causes a conformational change in the shape of Hemoglobin. This allows other O2 molecules to bind more easily in succession.

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11
Q

What is the composition of hemoglobin (Hb)?

A

4 subunits connected together, each with a heme group

Each subunit has a heme group that contains 1 iron atom in its center. It is the iron core that binds to oxygen.

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12
Q

What is the composition of myoglobin?

A

1 subunit with 1 heme group

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13
Q

What is the main difference between the oxygen carrying capacity of hemoglobin and myoglobin?

Basically where do they carry oxygen?

A

Hemoglobin: carries oxygen in the blood

Myoglobin: carries oxygen in the muscles

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14
Q

How many oxygen molecules can a single hemoglobin (Hb) molecule carry?

A

4 oxygen molecules

(1 in each heme group)

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15
Q

How many oxygen molecules can a single myoglobin molecule carry?

A

1 oxygen molecule

(1 heme group binds 1 oxygen molecule)

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16
Q

The majority of CO2 that enters the blood is absorbed and converted into carbonic acid which then dissociates. What does carbonic acid dissociate into?

A
  1. bicarbonate ion (HCO3-)
  2. hydrogen ion (H+)
17
Q

What is the equation for the bicarbonate buffer system in blood?

A
18
Q

If an oxyhemoglobin dissociation curve shifts towards the left, what kind of affinity does hemoglobin have for oxygen?

A

Hemoglobin has an increased affinity for oxygen.

_l_eft _l_oads O2 at the tissues”

19
Q

If an oxyhemoglobin dissociation curve shifts towards the right, what kind of affinity does hemoglobin have for oxygen?

A

Hemoglobin has decreased affinity for oxygen.

_r_ight _r_ids O2 into the tissues”

20
Q

[Mnemonic]

CADET, face right!

(how to remember which factors shift the oxygen-hemoglobin dissociation curve/Bohr effect to the right)

A

CADET, face right!

  • pCO2
  • Acidity (↓ pH, ↑ [H+])
  • 2,3- BPG (diphosphoglycerate)
  • Exercise
  • Temperature

An increase (NOT decrease) in ALL of these will shift the curve to the right.

21
Q

How do RBCs produce ATP?

A

Via anaerobic glycolysis

22
Q

RBCs have an enzyme called bisphosphoglycerate mutase. What is the function of this enzyme?

A

Converts 1,3-BPG (from glycolysis) to 2,3-BPG.

23
Q

What effect does 2,3-BPG have on adult hemoglobin (HbA)?

A

Binds allosterically and decreases HbA’s affinity for oxygen.

This causes a _r_ight shift in a oxyhemoglobin dissociation curve because HbA _r_ids of oxygen at the tissues.

24
Q

2,3-BPG ONLY binds to adult hemoglobin (HbA), but not to fetal hemoglobin (HbF). What effect does this have on HbF?

A

HbF can bind to oxygen and therefore has a higher affinity for oxygen than maternal HbA.