Pul 3 - Oxygen and Hemoglobin Flashcards

1
Q

What is the difference between T form of hemoglobin and R form of hemoglobin?

A

Called taut form, it has low affinity for oxygen, favoring tissue; delivering oxygen to tissue.

R form is called the relaxed form, it has a high affinity for oxygen.

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2
Q

What is positive cooperativity for hemoglobin?

A

It means that once hemoglobin is bound to one oxygen, it is more likely to bind to a second oxygen, and so on.

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3
Q

What is the cause of the S (sigmoid) shape of oxygen dissociation curve?

A

Positive cooperativity of hemoglobin to oxygen.

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4
Q

What favors the T form of hemoglobin?

A
  1. CO2
  2. Hydrogen Ion
  3. Increased temperature
  4. 2,3-DPG
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5
Q

What is the component of fetal hemoglobin?

A

It is made up of 2 alpha globins and 2 gamma globins.

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6
Q

What are some unique properties for fetal hemoglobins?

A

It has lower affinity for 2,3-DPG and higher affinity for O2.

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7
Q

How do we measure PO2 vs how do we measure hemoglobin saturation?

A

Partial pressure of oxygen is measured by an arterial blood gas (ABG). We can measure hemoglobin saturation with a pulse oxymeter.

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8
Q

How do we shift the oxygen-hemoglobin dissociation curve to the right?

A

Everything that that favors the change of hemoglobin to a T form; CO2, increase in 2,3-DPG, H+, Increase in temp.

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9
Q

How do we shift the oxygen-hemoglobin dissociation curve to the left?

A

Decreasing CO2, decreasing 2,3-DPG, alkalosis, decreasing tempature. Also, fetal hemoglobin is shifted to the left (lower affinity to 2,3-DPG).

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10
Q

What are two form of toxic hemoglobin?

A

Methemoglobin and carboxyhemoglobin.

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11
Q

What is methemoglobin?

A

It is the oxydized form of hemoglobin; it has iron in the ferric form (Fe3+: remember that ferric ends in “c”, the third letter of the alphabet). Ferrous is the Fe2+ (change the the last letter “s” in ferrous to a “2”).

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12
Q

What are the structural components of Hemoglobin (HbA)?

A

It is made up of 2 alpha globins and 2 beta globins; each globin is bound to a heme, making 4 heme oxygen binding site in one hemoglobin.

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13
Q

Methemoglobin has decreased affinity for oxygen but has increased affinity for what substance?

A

Methemoglobin has an increased affinity for cyanide.

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14
Q

What substance do we use to purposely oxidize hemoglobin to methemoglobin? And in what pathology can we use this to our advantage?

A

Nitrite and sodium nitrite change hemoglobin to methemoglobin. This can be used as an antidote to cyanide poisoning, so the methemoglobin can circulate in the body, picking up cyanide.

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15
Q

What are the components of a cyanide antidote kit?

A
  1. Amyl nitrite (inhaled).
  2. Sodium nitrite (IV).
    Then after some time:
  3. Thiosulfate: it binds to cyanide and forms thyocyanade, which then can be excreted by the kidneys.
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16
Q

What are the causes of methemoglobinemia?

A

They are caused by drugs.

  1. Nitrates and nitrites.
  2. Antimalarial drugs: Chloroquine, primaquine.
  3. Dapsone.
  4. Sulfonamides.
  5. Local anesthetics: lidocaine.
  6. Metoclopramide.
17
Q

What is the treatment for methemoglobinemia?

A
  1. Methylene blue.
  2. Vitamin C.
  3. Cimetidine (Gradually lowers it, so not for acute but people with chronic use of drugs that cause methemoglobinemia).
18
Q

What is carboxyhemoglobin?

A

Hemoglobin bound to carbomonoxide. It has an affinity of 250x greater than oxygen.

19
Q

What does carboxyhemoglobin cause?

A

Decrease in O2 binding capacity. Causes a leftward shift in O2-hemoglobin dissociation curve.

20
Q

Why is the use of pulse oxymeter detrimental in the case of carboxyhemoglobin poisoning cases?

A

Patient can have lots of carboxyhemoglobin but the pulse oxymeter will be normal because it only indicates hemoglobin saturation, not specifically for oxygen.

21
Q

Which for of hemoglobin has a high affinity for oxygen? Which form has low affinity for oxygen?

A

R form (relaxed) has high affinity for oxygen while T form (taut) has low affinity for oxygen.