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final exam > Chap 7 > Flashcards

Chap 7 Flashcards

Hemoglobin

1
Q

Adult Male and Female Hgb Reference Ranges are?

A

Males= 13.5-18.0 g/dL
Females= 12.0-15.0 g/dL

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2
Q

Newborn and Children Hgb Reference Ranges are?

A

Newborns= 16.5-21.5 g/dL
Children 8-13= 12.0-15.0 g/dL

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3
Q

Hemoglobin

A

Iron-bearing protein and the main component of RBCs.

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4
Q

Hemoglobin gives RBCs what?

A

Its color

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5
Q

During what stage of Erythrocyte maturation, does the majority of Hgb synthesis take place?

A

Rubricyte (Polychromatophilic Normoblast) Stage

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6
Q

What regulates the production of Hemoglobin?

A

Tissue hypoxia

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7
Q

Tissue hypoxia causes the kidneys to do what?

A

Increase production of EPO, which increases RBC and hemoglobin production.

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8
Q

Functions of Hgb?

A

Carry oxygen from lungs to tissues.
Remove CO2
Buffering Action

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9
Q

What is the buffering action of Hgb?

A

Maintains blood pH as it changes from Oxyhemoglobin (W/ Oxygen) to Deoxyhemoglobin (w/o Oxygen).

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10
Q

How many polypeptide subunits make up the Hgb structure?

A

4

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11
Q

The heme group of a hemoglobin molecule is made of?

A

Porphyrin Ring
Ferrous Iron (Reduced state, Fe 2+)

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12
Q

The globin chains in a NORMAL PT are?

A

2 Alpha Chains
2 Beta Chains

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13
Q

Heme Synthesis takes place where?

A

The mitochondria of developing RBCs in the BM.

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14
Q

What processes are necessary for normal Hgb Synthesis?

A

Adequate Iron supply & delivery
Adequate synthesis of protoporphyrins
Adequate globin synthesis

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15
Q

Transferrin

A

Iron transporter

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16
Q

Protoporphyrin synthesis occurs where?

A

Mitochondria of RBC precursors.

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17
Q

What mediates protoporphyrin synthesis?

A

EPO and Vitamin B-6

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18
Q

Protoporphyrin + Iron=?

A

Heme

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19
Q

Porphyrin synthesis is proportional to the rate or?

A

Globin Synthesis

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20
Q

What determines proper globin synthesis?

A

Genes

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21
Q

the precise order of Amino acids in globin chains is critical for?

A

Structure and function of Hemoglobin.

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22
Q

What are the globin chain designations?

A

a- Alpha

B- Beta

d- Delta

e- Epsilon

y- Gamma

Z- Zeta

23
Q

Embryonic Hemoglobins?

A

Gower-1
Gower-2
Portland

24
Q

Gower-1 Hb is made of which globin chains?

A

2- Zeta
2-Epsilon

25
Q

Gower-2 Hb is made of which globin chains?

A

2-Alpha
2-Epsilon

26
Q

Portland Hb is made of which globin chains?

A

2-Zeta
2- Gamma

27
Q

Fetal Hb is made of which globin chains?

A

2- Alpha
2-Gamma

28
Q

What are the adult Hemoglobins?

A

HB A
HB A2
HB F

29
Q

Hb A is made of which globin chains?

A

2- Alpha
2- Beta

30
Q

Hb A2 is made of which globin chains?

A

2-Alpha
2-Delta

31
Q

Hb F is made of which globin chains in adults?

A

2-Alpha
2-Gamma

32
Q

What is the incidence of Hb A in adults?

A

95%

33
Q

What is the incidence of Hb A2 in adults?

A

1.5-3.7%

34
Q

What is the incidence of Hb F in adults?

A

<2%

35
Q

Oxygen Affinity

A

The ease W/ which Hb binds and releases Oxygen.

36
Q

When Hb has an increased oxygen affinity?

A

Hb binds more oxygen and doesn’t want to let go. (Kind of like Rick Astley….never gonna let you down)

37
Q

Decreased Oxygen affinity?

A

Hb releases oxygen easier.

38
Q

What can cause a right shift of the oxygen disassociation curve?

A

Increased H+
Increased CO2
Increased Temp
Increased 2,3-BPG

39
Q

What can cause a left shift of the oxygen disassociation curve?

A

Decreased H+
Decreased CO2
Decrease in Temp
Decrease in 2,3-BPG

40
Q

Acidic blood pH shifts?

A

Curve shifts right

41
Q

Alkaline blood pH shifts?

A

Curve shifts left

42
Q

When pH effects the oxygen disassociation curve its called?

A

Bohr Effect

43
Q

A right shift means?

A

Hgb has less attraction to oxygen.
Hgb willing to release oxygen to tissues.
(I.E. Anemia, Acidosis)
Even W/ less RBCs, they act more efficiently to deliver oxygen to target.

44
Q

A left shift means?

A

Hgb attracted to Oxygen
Less willing to release oxygen to tissues.
(I.E. Abnormal Hgb or Alkalosis).

45
Q

Cyanosis

A

presence of > 5 g/dL deoxyhemoglobin in blood.
PTs appear blue

46
Q

3 abnormal Hemoglobins?

A

Methemoglobin
Carboxyhemoglobin
Sulfhemoglobin

47
Q

Methemoglobin could be caused by?

A

Hb M
Cytochrome b5 reductase deficiency

48
Q

What is Hb M?

A

An inherited autosomal dominant pattern, W/ methemoglobin comprising 30-50% of total Hb in the body.

49
Q

Sulfehemoglobin

A

an irreversible oxidation of Hb by drugs (Sulfanilamides, Phenacetin, Nitrites, Phenylhydrazine) or exposure to sulfur chemicals in an industry or environmental setting.

50
Q

Carboxyhemoglobin

A

combination of carbon monoxide W/ heme iron.

51
Q

What is Carbon Monoxide’s affinity for Hemoglobin?

A

240x that of oxygen

52
Q

Causes of carboxyhemoglobin?

A

Inhaling car exhaust
Tobacco Smokers
Industrial Pollutants (Gas, Coal, Charcoal)

53
Q
A

final exam (27 decks)

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