Hemoglobin Flashcards

1
Q

Hgb is aka

A

Respiratory pigment

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2
Q

concentration of Hb within RBCs:

A

approximately 34 g/dL

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3
Q

Hgb molecular weigh

A

approximately 64,000 Daltons

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4
Q

who identified the respiratory prote

A

Felix Seyler

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5
Q

1 gram of hemoglobin can carry _____ of oxygen

A

1.34 mL

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6
Q

1 gram of hemoglobin can carry a constant _____ iron

A

3.47 mg

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7
Q

hemoglobin components

A

1) globin
2) nitrogenous protoporphyrin IX
3) four heme molecules
4) one 2,3-BPG

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8
Q

Hemoglobins with 141 amino acids

A

Alpha & Zeta

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9
Q

Primary functions of hgb

A

1) To deliver oxygen to the tissues
2) To carry waste product CO2 away to the lungs
3) Binding, inactivation, and transport of NO (Nitric Oxide) = newly discovered function

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10
Q

Protein Structures of Hemoglobin

A

1) PRIMARY
2) SECONDARY
3) TERTIARY
4) QUATERNARY (TETRAMER)

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11
Q

measurement of hgb in the blood

A

HEMOGLOBINOMETRY

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12
Q

reference method of hemoglobinometry

A

Cyanmethemoglobin (HiCN) Method

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13
Q

reagent used in Cyanmethemoglobin (HiCN) Method

A

Drabkin’s reagent

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14
Q

major components of Drabkin’s reagent

A

Potassium ferricyanide (K3Fe(CN)6) & Potassium cyanide (KCN

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15
Q

Potassium ferricyanide function

A

converts hgb to methemoglobin

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16
Q

Potassium cyanide function

A

provides cyanide ions

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17
Q

HiCN is measured at

A

540 nm

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18
Q

(All types of Hb may be measured through HiCN except

A

sulfhemoglobin

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19
Q

Cyanmethemoglobin reagent stored in

A

brown bottle or in a dark place

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20
Q

r technique that has been used in some automated instruments involves the use of _____ to transform hgb to methemoglobin and does not produce toxic wastes

A

f sodium lauryl sulfate (SLS)

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21
Q

HEMOGLOBIN ELECTROPHORES is for

A

identifying hgb

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22
Q

movement of charged particles in an electric field

A

Electrophoresis

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23
Q

fastest abnormal hgb

A

Hgb H

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24
Q

fastest normal hgb

A

HbA1

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25
Q

slowest abnormal hgb

A

Hgb C, Hgb A2, Hgb E, HgbC harlem, Hgb O arab

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26
Q

citrate agar electrophoresis pH

A

pH 6.0 to 6.2

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27
Q

Cellulose acetate electrophoresis pH

A

pH 8.4 to 8.6

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28
Q

citrate agar electrophoresis is used as

A

complementary procedure to Cellulose acetate that further differentiates Hb S from Dand G, and Hb C from Hb E, O arab, C harlem

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29
Q

HEME a.k.a

A

. Ferroprotoporphyrin IX

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30
Q

Site of heme synthesis:

A

mitochondrion

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31
Q

heme synthesis occurs in

A

liver & bone marrow

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32
Q

Ferrochelatase aka

A

Heme synthetase

33
Q

Ferrochelatase function

A

enzyme neded to insert ferous iron to the protoporphyrin IX ring

34
Q

Master regulatory hormone of systemic iron metabolism

A

HEPCIDIN

35
Q

Processes involved in Iron metabolism

A

” AT USE I “

Absorption
Transportation
Utilization
Storage
Excretion
Iron recycling
36
Q

site of maximal absoprtion of iron

A

duodenum and upper jejunum

37
Q

ionic iron

A

ferrous

38
Q

non ionic iron

A

heme

39
Q

most dietary iron is what iron form

A

Ferric

40
Q

ferroportin function

A

delivers ferrous iron into the blood

41
Q

Hephaestin function

A

reoxidizes ferrous (Fe+2) into ferric (Fe+3) form as it exits for transport into the blood.

42
Q

apotransferrin function

A

transports iron in the blood

43
Q

Transferrin is

A

Apotransferrin with bound ferric (Fe+3) form of iron

44
Q

storage form of iron

A

ferritin

45
Q

most sensitive for IDA

A

Serum Ferritin

46
Q

partially degraded ferritin that appears in cases of iron overload

A

hemosiderin

47
Q

hemosiderin stain

A

Prussian blud

48
Q

when is iron recycled

A

when cells die

49
Q

most abundant in iron

A

RBCs

50
Q

also a plasma protein but is able

to save heme.

A

hemopexin & Haptoglobin

51
Q

Ferritin and hemosiderin mostly found in

A

macrophages and

hepatocytes

52
Q

body iron status tests

A

1) Serum iron
2) Total Iron binding capacity
3) Transferrin saturation
4) Serum ferritin
5) Prussian blue
6) free erythrocyte protoporphyrin

53
Q

considered the
gold standard for assessment of
body iron.

A

Prussian blue stain

54
Q

first laboratory test
to become abnormal when iron
stores begin to decline)

A

Serum Ferritin

55
Q

used for the differential diagnosis of

disorders of iron metabolism

A

serum iron

56
Q

indirectly measures the concentration
of transferrin by measuring its ability
to bind iron

A

Total Iron Binding Capacity

57
Q

Increased iron accumulation (blood and tissues)

A

1) HEMOSIDEROSIS

2) HEMOCHROMATOSIS

58
Q

-increased tissue iron stores without accompanying

tissue damage

A

HEMOSIDEROSIS

59
Q

increase in iron accumulation in body tissue leading to tissue damage

A

HEMOCHROMATOSIS

60
Q

Globin Synthesis site

A

ribosomes in the normoblast

61
Q

Chromosome 16 function

A

Dictates production of Alpha & Zeta globin chains

62
Q

Chromosome 11 function

A

dictates the production of other kinds of globin chains

63
Q

predominant form of Hgb in the fetus and newborn

A

Hgb F

64
Q

Hb F structure

A

2 Alpha + 2 Gamma

65
Q

Portland

A

2 zeta + 2 gamma

66
Q

gower I

A

2 Zeta + 2 eepsilon

67
Q

Gower II

A

2 ALPHA + 2 EPSILON

68
Q

Adult forms of hgb

A

1) Hb F
2) Hb A1
3) Hb A2

69
Q

predominant form of adult hemoglobin

A

Hgb A1

70
Q

Hgb A1

A

2 alpha + 1 beta

71
Q

Hgb A2

A

2 alpha + a delta

72
Q

hemoglobin derivatives

A

A. FUNCTIONAL HGB
1) oxyhemoglobin
2)deoxyhemoglobin
B. DYSHEMOGLOBINS

73
Q
  • Bright color
  • relaxed state
  • Hb w/ ferrous iron + Oxygen
A

Oxyhemoglobin

74
Q
  • Cherry red

- Hb w/ ferrous iron bound to CO

A

Carboxyhemoglobin

75
Q

silent killer

A

Carboxyhemoglobin

76
Q

Carboxyhemoglobin has ___ times greater affinity to Hb than oxygen

A

240 times

77
Q
  • chocolate brown

- Hb w/ FERRIC iron not bound to oxygen

A

Methemoglobin

78
Q

aka Ferrihemoglobin, hemiglobin

A

Methemoglobin

79
Q
  • mauve-lavender

- oxidized, partially denatured formscof Hb

A

Sulfhemglobin