Hemoglobin Flashcards

1
Q

iron bearing protein contained
within the erythrocytes

A

hemoglobin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

function of hemoglobin

A

Transport oxygen from the lungs
to the tissue and carbon dioxide
from the tissue.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

it is synthesized by young
erythroblast from the
polychromatophilic normoblast
stage up to reticulocytes stage

A

hemoglobin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Composition of Heme

A

Protophorphyrin IX
Ferrous iron

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

amino acids of alpha and zeta

A

141

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

amino acids of beta

A

146

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

pretzel like
configuration

A

tertiary

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

amino acid sequence

A

primary

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

complete molecule

A

quarternary

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

helices and non
helices

A

secondary

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Occurs in the cytoplasm of normoblast and
reticulocytes.

A

synthesis of globin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

manufactured in
the ribosomes

A

Polypepdtide chains

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

made via transcription
of m genetic code to mRNA and
translation of mRNA.

A

Globin protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

the ability of hemoglobin to bind or
release oxygen . Expressed in terms of the oxygen
tension at which hgb is 50% saturated

A

oxygen affinity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

The relationship between O2 tension and
hemoglobin saturation with oxygen is described as

A

OXYGEN DISSOCIATION
CURVE

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

relationship of O2 affinity with
Hb to pH

A

bohr effect

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

decreases oxygen affinity , more 02 release to the
tissues

A

right shift

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

increases oxygen affinity less 02 release to the
tissues

A

left shift

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

hemoglobin in combination with
oxygen.
gives pinkness to the skin and mucous membrane.
seen in arterial circulation

A

Oxyhemoglobin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

hgb with iron but no O2 seen in
venous circulation
unassociated with oxygen

A

Deoxyhemoglobin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Found in normal human embryos
and fetuses with a gestational age
of less than three months

Absent at birth

A

Embryonic Hemoglobin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Composed of 2 zeta and 2 epsilon globin
chains

A

Hemoglobin Gower I

23
Q

Composed of 2 alpha and 2 epsilon

A

Hemoglobin Gower 2

24
Q

composed of 2 zeta and 2 gamma

A

Hemoglobin Portland

25
the major hemoglobin of the fetus and newborns Composed 0f 2 alpha and 2 gamma Produced four months after conception
Fetal Hemoglobin ( HbF)
26
normal adult hemoglobin 95 to 97 %of hemoglobin in normal adults produced after one year onwards composed of 2 alpha (141 AA) and 2 beta chains(146 AA)
Hemoglobin A or A1
27
Constitutes less than 3% of the total hemoglobin Composed of 2 alpha and 2 delta
Hemoglobin A2
28
- degradation product of HbA2 - composed of 2 alpha and 2 delta
Hemoglobin A3
29
this is the primary hemoglobin in people with sickle cell disease. causes the red blood cell to deform and assume a sickle shape when exposed to decreased amounts of oxygen
Hemoglobin S
30
Glutamic acid is replaced by
valine in the 6th position of beta chain
31
It usually causes a minor amount of hemolytic anemia and a mild to moderate enlargement of the spleen About 2-3% of people of West African descent are heterozygotes for
hemoglobin C
32
is one of the most common beta chain hemoglobin variants in the world
Hemoglobin E
33
an abnormal hemoglobin that occurs in some cases of alpha thalassemia
hemoglobin H
34
Is a form hgb in its ferric state * Has a brownish to bluish color and does not revert to red on exposure to oxygen. * Peak in the range of 620 – 640 nm at pH 7.1 under spectral absorption test
METHEMOGLOBIN
35
Formed by the irreversible oxidation of Hb of certain drugs and chemicals Formed by the addition of hydrogen sulfide to hgb has a greenish pigment.
SULFHEMOGLOBIN
36
If sulfhemoglobin reaches the critical level in the blood it imparts
MAUVE LAVENDER
37
Results from the binding of carbon monoxide to heme iron. * Hb can combine with carbon monoxide with affinity 200 times greater than that of Oxygen.
CARBOXYHEMOGLOBIN
38
termed as silent killer for its colorless gas , odor and patient becomes easily hypoxic
Carbon monoxide.
39
qualitative screening test based on specific gravity. The density of the drop of blood is directly proportional to the amount of hemoglobin it contains
Copper Sulfate Specific Gravity
40
Hb will combine and liberate a fixed quantity of O₂. The blood is hemolyzed with saponin and the gas is collected and measured in a Van Slyke apparatus.
Gasometric Method (Oxygen Capacity Method)
41
when the drop of donor's blood dropped into copper sulfate solution becomes encased in a sac of copper proteinate, which prevents any change in the specific gravity for about 15 seconds
Copper Sulfate Specific Gravity
42
measures plasma hemoglobin
Oxyhemoglobin Method
43
Photoelectric
- Oxyhemoglobin Method - Cyanmethemoglobin or HiCN method
44
Colorimetric Methods
- Visual - Photoelectric
45
Blood is diluted in a solution of potassium ferricyanide and potassium cyanide. The hemoglobin is oxidized to methemoglobin by the potassium ferricyanide.
Cyanmethemoglobin or HiCN method
46
reagent used in hemoglobin determination - pale and yellow with a pH of 7.2 +0.2
Modified drabkin’s reagent
47
Reference Range for cyanmethemoglobin
M: 13.5-18 g/dL F: 12-15 g/dL
48
decreased hemoglobin level
oligochromia
49
People living at high altitudes
increased Hb values
50
Excessive fluid intake
decrease hb
51
during pregnancy
decrease hb
52
The panic Hb is less than 5.0 g/dl a conditions that leads to
heart condition and death
53
A value more than 20 g/dl leads to
clogging of the capillaries as a result of hemoconcentration