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HEMA 1 LEC > Chapter 4 - HEMOGLOBIN (Functions, Components, Synthesis, Types, Forms) > Flashcards

Chapter 4 - HEMOGLOBIN (Functions, Components, Synthesis, Types, Forms) Flashcards

1
Q

Respiratory pigment found in the red cells

A

HEMOGLOBIN

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2
Q

A conjugated protein synthesized in the RBCS

A

HEMOGLOBIN

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3
Q

It represents more than 1% of the total body weight and It occupies 28% of the red cell mass.

A

HEMOGLOBIN

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4
Q

HEMOGLOBIN Function:

A

Transports oxygen from the lungs where the oxygen tension is high, to the tissues, where the oxygen tension is low.

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5
Q

HEMOGLOBIN also binds to other substances such as (?).

A

hydrogen ions (which determine pH of the blood), carbon dioxide and 2,3 diphosphoglycerate (2,3-DPG)

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6
Q

These substances do not bind to hemoglobin at the oxygen-binding sites, however, binding of these substances to hemoglobin affects the (?).

A

affinity of hemoglobin to oxygen

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7
Q

Conversely, binding of (?) causes changes in the structure of the hemoglobin molecule thus affecting its ability to bind other gases or substances

A

oxygen to hemoglobin

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8
Q

How is CO2 transported in the blood (plasma and red cells?)

A
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9
Q

As CO2 enters the blood, it combines with H2O to form (?), a relatively weak acid, which dissociates into (?).

A

carbonic acid (H2CO3)

H+ and HCO3 -

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10
Q

Blood acidity is minimally affected by the released (?)because blood proteins, especially hemoglobin, are effective buffering agents.

A

H+ ions

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11
Q

The conversion of CO2 to H2CO3 is catalyzed by (?), an enzyme present inside the RBCs.

A

carbonic anhydrase

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12
Q

Because the enzyme is present only in the RBCs, (?) accumulates to a much greater extent within the red cells than in the plasma.

A

HCO3

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13
Q

The capacity of blood to carry (?) - is enhanced by an ion transport system inside the RBC membrane that simultaneously moves a HCO3 - out of the cell and in exchange for a chloride ion.

A

CO2 as HCO3

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14
Q

The simultaneous exchange of these 2 ions, known as the (?), permits the plasma to be used as a storage site for bicarbonate without changing the electrical charge of either the plasma or the red blood cell.

A

chloride shift

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15
Q

is a curve that plots the proportion of hemoglobin in its saturated form on the Y axis against the prevailing oxygen tension on the X axis.

A

oxygen dissociation curve/oxyhemoglobin dissociation curve (ODC)

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16
Q

This relates oxygen saturation and partial pressure of O2 in the blood (PO2)

A

oxygen dissociation curve/oxyhemoglobin dissociation curve (ODC)

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17
Q

determined by hemoglobin affinity for oxygen.

A

oxygen dissociation curve/oxyhemoglobin dissociation curve (ODC)

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18
Q

Explain the influence/effect of Bohr effect, Haldane effect, 2, 3, DPG and chloride on the affinity of hemoglobin to oxygen

A
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19
Q

Blood temp

A
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20
Q

Blood pH (Bohr Effect)

A
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21
Q

RBC 2,3 DPG

A
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22
Q

CO2 (Haldane Effect)

A
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23
Q

Hb F

A
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24
Q

Abnormal Hbs

A
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25
Q

HEMOGLOBIN COMPOSITION:

A
  1. 1 Globin
  2. 4 Heme
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26
Q

inorganic iron groups that assist in binding O2

A

Heme

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27
Q

each iron atom can bind and then release an oxygen molecule

A

Heme

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28
Q

nitrogenous substance formed in the mitochondrion

A

Protoporphyrin IX

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29
Q

a salt produced in the Rapoport-Luebering shunt in the RBCs.

A

2,3 Diphosphoglycerate (DPG)

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30
Q

Composed of 2 sets (dimer) of 2 different polypeptide chains

A

GLOBIN Chains

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31
Q

The spatial arrangement of each alpha-beta pair is symmetrical

A

GLOBIN Chains

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32
Q

Contacts between the subunits are by means of H-bonds

A

GLOBIN Chains

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33
Q

Differences in the globin chain relate both to the sequence and to the number of amino acids in the chain.

A

GLOBIN Chains

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34
Q

141

A

Alpha

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35
Q

Beta
Delta
Gamma
Epsilon

A

146

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36
Q

Gower-1

A

2 zeta 2 epsilon

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37
Q

Gower-2

A

2 alpha 2 epsilon

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38
Q

Portland

A

2 zeta 2 gamma

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39
Q

Hb A

A

2 alpha 2 beta

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40
Q

Hb A2

A

2 alpha 2 delta

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41
Q

Hb F

A

2 alpha 2 gamma

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42
Q

TYPES OF HEMOGLOBIN

A
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43
Q

: Major normal adult hemoglobin (97%)

A

Hb A1

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44
Q

: Major Hb of the fetus and the newborn

A

Hb F

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45
Q

Has high affinity to O2

A

Hb F

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46
Q

Resistant to both acid elution and alkali denaturation

A

Hb F

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47
Q

After birth, smaller amounts of(?) are produced

A

HbF

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48
Q

= HbF is less than 8%

A

6 months

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49
Q

= HbF less than 2%

A

After age 2 years

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50
Q

= less than 1%

A

Adults

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51
Q

Accounts for 1.5 % - 3.5 % of normal adult Hb

A

Hb A2

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52
Q

Increased in some -Thalassemias, hyperthyroidism and in some cases of megaloblastic anemia

A

Hb A2

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53
Q

= analogue of alpha-chain

A

zeta chain

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54
Q

= counterpart of the gamma, beta, and delta chains

A

epsilon chain

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55
Q

EMBRYONIC HEMOGLOBINS

A

Hb Gower I
Hb Gower II
Hb Portland

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56
Q

FORMS of HEMOGLOBIN

NORMAL

ABNORMAL

A
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57
Q

Formed when the RBCs pass through the alveolar capillaries of the lungs

A

Oxyhemoglobin (HbO2)

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58
Q

The O2 is loosely bound and unstable for easier release into the tissues

A

Oxyhemoglobin (HbO2)

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59
Q

Gives a scarlet red/bright red color

A

Oxyhemoglobin (HbO2)

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60
Q

Reduced form

A

Deoxyhemoglobin (HbCO2)

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61
Q

Hemoglobin with CO2 (carbaminohemoglobin)

A

Deoxyhemoglobin (HbCO2)

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62
Q

Gives a dark red color

A

Deoxyhemoglobin (HbCO2)

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63
Q

Hemoglobin with CO (affinity of CO to hb is 200 x greater than the affinity of O2)

A

Carboxyhemoglobin (HbCO)

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64
Q

Imparts a cherry red in color

A

Carboxyhemoglobin (HbCO)

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65
Q

Absorption wavelength: 576 nm

A

Carboxyhemoglobin (HbCO)

66
Q

Critical Value: 5g /100 ml (May cause irreversible tissue changes when increased)

A

Carboxyhemoglobin (HbCO)

67
Q

Treatment: administration of hyperbaric O2

A

Carboxyhemoglobin (HbCO)

68
Q

Rapid Tests for HbCO :

A
  1. NaOH test: red color
  2. Dilution test (addition of water): cherry red
  3. Tannic Acid test: red precipitate
69
Q

: red color
: cherry red
: red precipitate

A
  1. NaOH test
  2. Dilution test (addition of water)
  3. Tannic Acid test
70
Q

Iron (Fe++) is oxidized into its Fe+++ form

A

Methemoglobin/Hemiglobin (Hi)

71
Q

Normally makes up 1.5%

A

Methemoglobin/Hemiglobin (Hi)

72
Q

Approximately 0.5% - 3% of the total body Hb is spontaneously converted to Hi daily

A

Methemoglobin/Hemiglobin (Hi)

73
Q

Conveys a chocolate brown color

A

Methemoglobin/Hemiglobin (Hi)

74
Q

Absorption wavelength: 630 635 nm

A

Methemoglobin/Hemiglobin (Hi)

75
Q

Methemoglobin/Hemiglobin (Hi)

Screening tests:

A

Aeration: blood retains its color
Addition of 1% MB: blood turns red

76
Q

Maintenance of Hemoglobin in the Normal Reduced state (Fe++):

Production of

reduced (?) in the presence of methemoglobin reductase (diaphorase)

reduced (?) in the presence of Glucose-6-PO4 dehydrogenase

(?) and its associated enzymes

A

Diphosphopyridine dinucleotide (DPNH)

Triphosphopyridine nucleotide (TPNH)

Glutathione

77
Q

: blood retains its color
: blood turns red

A

Aeration

Addition of 1% MB

78
Q

Conditions of Methemoglobinemia:

A
79
Q

: commonly attributed to NADH-Methemoglobin reductase deficiency/Diaphorase deficiency

A

a. Inherited (enzyme deficiency)

80
Q

: results of various amino acid substitutions in the globin chain that directly affect the heme group.

A

b. Inherited M

81
Q

: effects of chemical or therapeutic agents (aniline dyes, nitrate-rich water and foodstuffs)

A

c. Acquired

82
Q

Formed when organic sulfides combine with Hb

A

Sulfhemoglobin (SHb)

83
Q

Observed in patients taking in oxidant drugs (phenacetin & acetanilid, sulfonamides)

A

Sulfhemoglobin (SHb)

84
Q

Irreversible once formed

A

Sulfhemoglobin (SHb)

85
Q

NOT normally present in the blood

A

Sulfhemoglobin (SHb)

86
Q

Imparts a greenish color

A

Sulfhemoglobin (SHb)

87
Q

Absorption wavelength: 600 - 620 nm

A

Sulfhemoglobin (SHb)

88
Q

Reference Values for Hemoglobin

Male:
Female:
At Birth:

A

140 175 g/L

123 153 g/L

150 200 g/L

89
Q

Increased Hb

A

Polycythemia Dehydration

90
Q

Decreased Hb

A

All anemia
Leukemia
Oligochromia

91
Q

Physiologic Variations:
After 50 years of age = (?)
Higher in the (?) and lower in the (?)
Lower if (?)
Increased in (?); high altitude

A

slight decrease

morning; evening

lying down

smokers

92
Q

Other forms of Hemoglobin:

A
93
Q

Formed when ferricyanide is added to the Fe++ of a normal Hb

A

Cyanmethemoglobin

94
Q

The most stable among the Hb pigments

A

Cyanmethemoglobin

95
Q

Absorption wavelength: 540 nm

A

Cyanmethemoglobin

96
Q

What are the glycosylated hemoglobins?

A
97
Q

is elevated 2 3 folds in patients with diabetes mellitus.

A

Hb AIc

98
Q

It is used as an index of metabolic control in diabetes during the preceding 2 - 3 mons.

A

Hb AIc

99
Q

Disorders Related with Abnormal Hemoglobins

A
100
Q

diverse group of genetic disorders characterized by a primary, quantitative reduction in globin chain synthesis for hemoglobin.

A

THALASSEMIA

101
Q
  1. Silent carrier
A

Alpha Thalassemia

102
Q
  1. Thalassemia trait/A-Thal minor
A

Alpha Thalassemia

103
Q
  1. Hb H disease
A

Alpha Thalassemia

104
Q
  1. Barts Hdrops fetalis
A

Alpha Thalassemia

105
Q
  1. Beta Thalassemia Major/Cooles anemia
A

Beta Thalassemias

106
Q
  1. Beta Thalassemia Intermedia
A

Beta Thalassemias

107
Q
  1. Beta Thalassemia Minor/Cooles trait
A

Beta Thalassemias

108
Q

conditions characterized by qualitative structural abnormalities of the globin polypeptide chains that result from alteration of the DNA genetic code for those chains

A

HEMOGLOBINOPATHIES

109
Q

Structural abnormalities may involve amino acid

A

HEMOGLOBINOPATHIES

110
Q

HEMOGLOBINOPATHIES (hemoglobin variants)

A
  1. Substitution
  2. Deletion
  3. Fusion
  4. Elongation
111
Q

Examples with Nomenclature:

  1. Substitution
  2. Deletion
  3. Fusion
  4. Elongation
A
112
Q

The most well-known hb variant characterized by substitution of glutamic acid by valine on the 6th amino acid posiion of he b-chain.

A

Hb S (Sicking hb)

113
Q

What are the effects of the glutamic acid substitution by valine on the 6th position of the β-chain in the Hb S molecule?

A
114
Q

Read the sickle cell crises. Be able to enumerate and discuss them.

A
115
Q

FUNCTIONAL CLASSIFICATION OF HEMOGLOBIN VARIANTS

A
116
Q

Hb M Boston a258Tyrb2

A

Hemoglobins associated with methemoglobinemia and cyanosis

117
Q

Hb M Iwate 287Tyr2

A

Hemoglobins associated with methemoglobinemia and cyanosis

118
Q

Hb M Saskatoon 2263Tyr

A

Hemoglobins associated with methemoglobinemia and cyanosis

119
Q

Hb M Milwaukee 2267Glu

A

Hemoglobins associated with methemoglobinemia and cyanosis

120
Q

Hb M Hde Park 2292Tyr

A

Hemoglobins associated with methemoglobinemia and cyanosis

121
Q

Hb FM Osaka 2263Tyr

A

Hemoglobins associated with methemoglobinemia and cyanosis

122
Q

Hb FM Fort Riple 2292Tyr

A

Hemoglobins associated with methemoglobinemia and cyanosis

123
Q

Hb Chesapeake 292Leu2

A

Hemoglobins associated with Increased Oxygen affinity and polycythemia

124
Q

Hb J Capetown 292Gln2

A

Hemoglobins associated with Increased Oxygen affinity and polycythemia

125
Q

Hb Malmo 2297Gln

A

Hemoglobins associated with Increased Oxygen affinity and polycythemia

126
Q

Hb Yakima 2299His

A

Hemoglobins associated with Increased Oxygen affinity and polycythemia

127
Q

Hb Kempse 2299Asn

A

Hemoglobins associated with Increased Oxygen affinity and polycythemia

128
Q

Hb Y psi (Ypsilanti) 2299Tyr

A

Hemoglobins associated with Increased Oxygen affinity and polycythemia

129
Q

Hb Hiroshima 22146Asp

A

Hemoglobins associated with Increased Oxygen affinity and polycythemia

130
Q

Hb Rainier 22145Cys

A

Hemoglobins associated with Increased Oxygen affinity and polycythemia

131
Q

Hb Bethesda 22145His

A

Hemoglobins associated with Increased Oxygen affinity and polycythemia

132
Q

Hb Kansas 22102Thr

A

Hemoglobins associated with Decreased Oxygen affinity and polycythemia

133
Q

Hb Titusville 294Asn2

A

Hemoglobins associated with Decreased Oxygen affinity and polycythemia

134
Q

Hb Providence 2282Asn

A

Hemoglobins associated with Decreased Oxygen affinity and polycythemia

135
Q

Hb Agenogi 2290Lys

A

Hemoglobins associated with Decreased Oxygen affinity and polycythemia

136
Q

Hb Beth Israel 22102Ser

A

Hemoglobins associated with Decreased Oxygen affinity and polycythemia

137
Q

Hb Yoshiuka 22108Asp

A

Hemoglobins associated with Decreased Oxygen affinity and polycythemia

138
Q

Hb Bibba 2136Pro2

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

139
Q

Hb Hammersmith 2242Ser

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

140
Q

Hb Bristol 2267Asp

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

141
Q

Hb Olmsted 22141Arg

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

142
Q

Hb Torino 243Val2

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

143
Q

Hb Ann Arbor 280Arg2

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

144
Q

Hb Genova 2228Pro

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

145
Q

Hb Shepherd’s Bush 2274Asp

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

146
Q

Hb Koln 2298Met

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

147
Q

Hb Wein 22130Asp

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

148
Q

Hb L-Ferrara 247Gly2

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

149
Q

Hb Hasharon 247His2

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

150
Q

Hb Leiden 226 or 7 (Glu deleted)

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

151
Q

Hb Freiburg 2223 (Val deleted)

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

152
Q

Hb Louisville 2242Leu

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

153
Q

Hb Seattle 2270Asp

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

154
Q

Hb Zurich 2263Arg

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

155
Q

Hb Gun Hill 2291-97 (5 a. a. deleted)

A

Hb may precipitate as Heinz bodies after splenectomy: “congenital Heinz body anemia”

156
Q

Hb Bart’s 4

A

Tetramers of normal chains

157
Q

Hb H 4

A

Tetramers of normal chains

158
Q

Hb S (Sicking hb)

A

Substitution

159
Q

Hb Gun Hil

A

Deletion

160
Q

Hb Constant Spring

A

Elongation

161
Q

Hb Lepore-Baltimore

A

Fusion

HEMA 1 LEC (15 decks)

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