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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
Describes the complete hemoglobin molecule
Tetramer
26
Occurs in most body cells except for mature erythrocytes
Heme biosynthesis
27
Predominant heme (porphyrin) producers
Red bone marrow and liver
28
Heme biosynthesis occurs in the
Mitochondria and cytoplasm of bone marrow erythroid precursors
29
Begins with condensation of _________ forming aminolevulinic acid (ALA) in a reaction catalyzed by ALA synthase
glycine and succinyl coenzyme A
30
added catalyzed by ferrochelatase to form HEME.
Ferrous ion
31
Globin synthesis starts at
3rd week of gestation.
32
Transcription of globin gene to mRNA occurs in the nucleus and translation of mRNA to the globin polypeptide chain occurs on
ribosome in the cytoplasm
33
has + charge and has highest affinity.
α chain
34
has the next highest affinity, followed by the delta-globin chain.
gamma-globin chain
35
major form in adults and children over 7 months.
HbA1
36
minor form of Hb in adults. It forms only 2 – 3% of a total Hb A.
HbA2 (2 α, 2 δ)
37
2 α and 2 γ subunits in fetus and newborn infant,
Fetal Hb (Hb F)
38
oxygenated hemoglobin
Oxyhemoglobin
39
deoxygenated hemoglobin
Deoxyhemoglobin
40
Reference intervals for hemoglobin concentrations Men
13.5-18.0 g/dL (135-180 g/L)
41
Reference intervals for hemoglobin concentrations: Women
12.0-15.0 g/dL (120-150 g/L)
42
Reference intervals for hemoglobin concentrations: Newborns
16.5-21.5 g/dL (165-215 g/L)
43
The shape of the curve is _______; this is due to cooperative binding of oxygen to hemoglobin.
sigmoidal
44
describes the relationship between partial pressure of oxygen (x axis) and the oxygen saturation (y axis).
oxygen-hemoglobin dissociation curve
45
few hemoglobin proteins have bound any oxygen.
At low oxygen partial pressure (PO2)
46
the number of hemoglobin proteins that have bound oxygen and the amount of oxygen that is bound rapidly increase, resulting in a sigmoidal curve
PO2 increases
47
What shift has a higher affinity for O2 – the hemoglobin of these species binds O2 more easily.
left-shifted ODC
48
helps describe the Hb-O2 affinity; it is the partial pressure of O2 at which 50% of all hemoglobin molecules have bound oxygen
P50
49
describes a lower affinity for hemoglobin and oxygen
higher P50
50
describes a higher affinity; oxygen will bind more easily to a hemoglobin
lower P50
51
The normal position of curve depends on
Concentration of 2,3-BPG •H+ ion concentration (pH) • CO2 in red blood cells •Structure of hemoglobin
52
Shift to the right
•High 2,3-BPG •High H+ •High CO2 •HbS
53
Carbon dioxide transport is facilitated by the RBC enzyme known as
carbonic ahydrase
54
Dysfunctional hemoglobins that are unable to transport oxygen
DYSHEMOGLOBINS
55
Dyshemoglobins include:
Methemoglobin Sulfhemoglobin Carboxyhemoglobin
56
contains Fe3+ instead of Fe2+ in heme groups.
Methemoglobin
57
If methemoglobin level increases to more than 30% what occurs
cyanosis and symptoms of hypoxia
58
is formed by irreversible oxidation of hemoglobin by drugs (such as sulfanilamides, phenacetin, nitrites and phenylhydrazine)
Sulfhemoglobin
59
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
Carboxyhemoglobin (COHb)
60
CO2 is non-covalently bound to globin chain of Hb. HbCO2 transports carbon dioxide in blood (about 23%).
Carbaminohemoglobin (HbCO2)
61
is formed spontaneously by nonenzymatic reaction with glycogen. People with diabetes mellitus have more HbA1c than normal (>7%).
Glycohemoglobin (HbA1c)
62
Normal counts of RBC in male
4.7 to 6.1 million cells per microliter (cells/mcL)
63
Normal counts of RBC in female
4.2 to 5.4 million cells per microliter (cells/mcL)
64
Volume and mean volume of RBC
80 to 100 fL and a mean volume of 90 fL.
65
Surface area of RBC membrane
140 um2
66
RBC is impermeable to
Sodium, potassium, and calcium
67
RBC is permeable to
Water, bicarbonate, and chloride
68
is a transmembrane protein that forms pores or channels whose surface charges create inward water flow in response to internal osmotic changes.
Aquaporin 1
69
also known as hexose monophosphate shunt
Hexose monophosphate pathway (HMP)
70
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.
Hexose monophosphate pathway (HMP)
71
extends the functional life span of the RBC by maintaining membrane proteins and lipids, enzymes, and hemoglobin iron in the functional, reduced, ferrous state.
Hexose monophosphate pathway (HMP)
72
The reduction of methemoglobin by NADPH is rendered more efficient in the presence of
methemoglobin reductase, also called cytochrome b5 reductase
73
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.
Methemoglobin reductase pathway
74
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.
Rapoport-Luebering pathway
75
anaerobic pathway; metabolizes glucose to pyruvate, consuming 2- ATP molecules. Thus, providing energy using kreb’s cycle.
Embden-Meyerhof pathway (EMP)

Hematology (28 decks)

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