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Hematology > Hemoglobin > Flashcards

Hemoglobin Flashcards

1
Q

It comprises approximately 95% of the cytoplasmic content of RBCs

A

hemoglobin

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2
Q

Provides protection from denaturation in the plasma and loss through the kindeys

A

Hemoglobin

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3
Q

Hemoglobin concentration and molecular weight

A

34 g/dL
64,000 daltons

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4
Q

Transport oxygen from the lungs to tissues and transport carbon dioxide from the tissues to the lungs for exhalation

A

Hemoglobin

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5
Q

Contributes to acid-base balance by binding and releasing hydrogen ions and transport nitric oxide, a regulator of vascular tone

A

Hemoglobin

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6
Q

Hemoglobin is a globular protein consisting of

A

Two different pairs of polypeptide chains and four heme group

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7
Q

Consists of a ring of carbon, hydrogen and nitrogen atoms (Protoporphyrin X) with a central atom of divalent ferrous iron

A

Heme

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8
Q

Oxidized hemoglobin

A

Methemoglobin

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9
Q

Designated A to H, contain subgroup numberings for the sequence of the amino acids in each helix and relatively rigid and linear

A

Helices

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10
Q

Connects the helices as reflected by their designations

A

Flexible nonhelical segments

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11
Q

Number of amino acids:

Alpha

A

141

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12
Q

Number of amino acids:

Beta

A

146

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13
Q

Number of amino acids:

Gamma A

A

146 (position 136; alanine)

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14
Q

Number of amino acids:

Gamma G

A

146 (position 136; glycine)

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15
Q

Number of amino acids:

Delta

A

146

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16
Q

Number of amino acids:

Epsilon

A

146

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17
Q

Number of amino acids:

Zeta

A

141

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18
Q

Number of amino acids:

Theta

A

Unknown

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19
Q

Refers to the amino acid sequence of the polypeptide chains

A

Primary structure

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20
Q

Refers to chain arrangements in helices and nonhelices

A

Secondary structure

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21
Q

Refers to the arrangement of the helices into a pretzel-like configuration

A

Tertiary structure

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22
Q

Globin chain amino acids in the cleft are

A

Hydrophobic

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23
Q

Amino acids outside the cleft are

A

Hydrophilic

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24
Q

Also called a tetramer

A

Quaternary structure

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25
Q

Describes the complete hemoglobin molecule

A

Tetramer

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26
Q

Occurs in most body cells except for mature erythrocytes

A

Heme biosynthesis

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27
Q

Predominant heme (porphyrin) producers

A

Red bone marrow and liver

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28
Q

Heme biosynthesis occurs in the

A

Mitochondria and cytoplasm of bone marrow erythroid precursors

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29
Q

Begins with condensation of _________ forming aminolevulinic acid (ALA) in a reaction catalyzed by ALA synthase

A

glycine and succinyl coenzyme A

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30
Q

added catalyzed by ferrochelatase to form HEME.

A

Ferrous ion

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31
Q

Globin synthesis starts at

A

3rd week of gestation.

32
Q

Transcription of globin gene to mRNA occurs in the nucleus and translation of mRNA to the globin polypeptide chain occurs on

A

ribosome in the cytoplasm

33
Q

has + charge and has highest affinity.

A

α chain

34
Q

has the next highest affinity, followed by the delta-globin chain.

A

gamma-globin chain

35
Q

major form in adults and children over 7 months.

A

HbA1

36
Q

minor form of Hb in adults. It forms only 2 – 3% of a total Hb A.

A

HbA2 (2 α, 2 δ)

37
Q

2 α and 2 γ subunits in fetus and newborn infant,

A

Fetal Hb (Hb F)

38
Q

oxygenated hemoglobin

A

Oxyhemoglobin

39
Q

deoxygenated hemoglobin

A

Deoxyhemoglobin

40
Q

Reference intervals for hemoglobin concentrations

Men

A

13.5-18.0 g/dL (135-180 g/L)

41
Q

Reference intervals for hemoglobin concentrations:

Women

A

12.0-15.0 g/dL (120-150 g/L)

42
Q

Reference intervals for hemoglobin concentrations:

Newborns

A

16.5-21.5 g/dL (165-215 g/L)

43
Q

The shape of the curve is _______; this is due to
cooperative binding of oxygen to hemoglobin.

A

sigmoidal

44
Q

describes the relationship between partial pressure of oxygen (x axis) and the oxygen saturation (y axis).

A

oxygen-hemoglobin dissociation curve

45
Q

few hemoglobin proteins have bound any oxygen.

A

At low oxygen partial pressure (PO2)

46
Q

the number of hemoglobin proteins that have bound oxygen and the amount of oxygen that is bound rapidly increase, resulting in a sigmoidal curve

A

PO2 increases

47
Q

What shift has a higher affinity for O2 – the hemoglobin of these species binds O2 more easily.

A

left-shifted ODC

48
Q

helps describe the Hb-O2 affinity; it is the partial pressure of O2 at which 50% of all hemoglobin molecules have bound oxygen

A

P50

49
Q

describes a lower affinity for hemoglobin and oxygen

A

higher P50

50
Q

describes a higher affinity; oxygen will bind more easily to a hemoglobin

A

lower P50

51
Q

The normal position of curve depends on

A

Concentration of 2,3-BPG
•H+ ion concentration (pH)
• CO2 in red blood cells
•Structure of hemoglobin

52
Q

Shift to the right

A

•High 2,3-BPG
•High H+
•High CO2
•HbS

53
Q

Carbon dioxide transport is facilitated by the RBC enzyme known as

A

carbonic ahydrase

54
Q

Dysfunctional hemoglobins that are unable to transport oxygen

A

DYSHEMOGLOBINS

55
Q

Dyshemoglobins include:

A

Methemoglobin
Sulfhemoglobin
Carboxyhemoglobin

56
Q

contains Fe3+ instead of Fe2+ in heme groups.

A

Methemoglobin

57
Q

If methemoglobin level increases to more than 30% what occurs

A

cyanosis and symptoms of hypoxia

58
Q

is formed by irreversible oxidation of hemoglobin by drugs (such as sulfanilamides, phenacetin, nitrites and phenylhydrazine)

A

Sulfhemoglobin

59
Q

results from combination of carbon monoxide with heme iron. It causes the ODC to the left, further increasing its affinity and severely impairing release of oxygen to the issues

A

Carboxyhemoglobin (COHb)

60
Q

CO2 is non-covalently bound to globin chain of Hb. HbCO2 transports carbon dioxide in blood (about 23%).

A

Carbaminohemoglobin (HbCO2)

61
Q

is formed spontaneously by nonenzymatic reaction with glycogen. People with diabetes mellitus have more HbA1c than normal (>7%).

A

Glycohemoglobin (HbA1c)

62
Q

Normal counts of RBC in male

A

4.7 to 6.1 million cells per microliter (cells/mcL)

63
Q

Normal counts of RBC in female

A

4.2 to 5.4 million cells per microliter (cells/mcL)

64
Q

Volume and mean volume of RBC

A

80 to 100 fL and a mean volume of 90 fL.

65
Q

Surface area of RBC membrane

A

140 um2

66
Q

RBC is impermeable to

A

Sodium, potassium, and calcium

67
Q

RBC is permeable to

A

Water, bicarbonate, and chloride

68
Q

is a transmembrane protein that forms pores or channels whose surface charges create inward water flow in response to internal osmotic changes.

A

Aquaporin 1

69
Q

also known as hexose monophosphate shunt

A

Hexose monophosphate pathway (HMP)

70
Q

detoxifies peroxide (H2O2), which arises from O2 reduction in the cell’s aqueous environment. H2O2 oxidizes heme iron to the non-functional ferric state and oxidizes and denatures proteins and lipids.

A

Hexose monophosphate pathway (HMP)

71
Q

extends the functional life span of the RBC by maintaining membrane proteins and lipids, enzymes, and hemoglobin iron in the functional, reduced, ferrous state.

A

Hexose monophosphate pathway (HMP)

72
Q

The reduction of methemoglobin by NADPH is rendered more efficient in the presence of

A

methemoglobin reductase, also called cytochrome b5 reductase

73
Q

Using H1 from NADH formed when G3P is converted to 1,3-BPG, cytochrome b5 reductase acts as an intermediate electron carrier, returning the oxidized ferric iron to its ferrous, oxygen-carrying state.

A

Methemoglobin reductase pathway

74
Q

A third metabolic shunt generates 2,3-bisphosphoglycerate (2,3-BPG; also called 2,3-diphosphoglycerate or 2,3-DPG). It enhances oxygen delivery to tissues.

A

Rapoport-Luebering pathway

75
Q

anaerobic pathway; metabolizes glucose to pyruvate, consuming 2- ATP molecules. Thus, providing energy using kreb’s cycle.

A

Embden-Meyerhof pathway (EMP)

Hematology (28 decks)

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