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HEMA LEC > Hemoglobin > Flashcards

Hemoglobin Flashcards

1
Q

to An iron bearing protein contained within the erythrocytes

A

Hemoglobin

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2
Q

The hemoglobin is synthesized by ______ and ________ stage up to reticulocytes stage

A

young erythroblast & polychromatophilic normoblast

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3
Q

a one gram of Hgb can carry how many ml of oxygen

A

1.34 ml

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4
Q

what are the composition of heme?

A

Protophorphyrin IX, Ferrous iron

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5
Q

What compose the 4 globin structure

A

2 identical pairs of unlike polypeptide chains, 141 to 146 amino acids each

each globin - 8 helices separated by 7 non helices segments

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6
Q

number of amino acids of Alpha & Zeta

A

141

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7
Q

Complete hemoglobin molecule described by?

A

Primary- amino acid sequence
secondary - helices and non helices
tertiary - pretzel like config.
quaternary - complete molecule

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8
Q

Occurs in the cytoplasm of normoblast and reticulocytes

A

Globin

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9
Q

It is manufactured in the ribosomes

A

polypeptide chains

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10
Q

It is made via transcription of m gen. code to mRNA and translation of mRNA

A

Globin protein

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11
Q

true or false: The third function of hemoglobin involves the binding, inactivation, and transport of nitric oxide.

A

true

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12
Q

It is secreted by vascular endothelial cells and causes relaxation of vascular wall smooth muscle and vasodilation

A

Nitric oxide

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13
Q

is 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

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14
Q

true or false: The relationship between O2 tension and hemoglobin saturation with oxygen is described as ODC

A

true

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15
Q

it is a relationship of O2 affinity with Hb to pH which states that :

Inc pH ( alkalosis) = Inc Hb affinity for O2

Dec pH ( acidosis )= dec hb affinity for O2

A

Bohr effect

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16
Q

Modified true or false :

Inc pH ( alkalosis)= dec Hb affinity for O2

Dec pH ( acidosis )= inc hb affinity for O2

A

both false

Inc pH ( alkalosis)= Inc Hb affinity for O2
Dec pH ( acidosis )= dec hb affinity for O2

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17
Q

Shift to the left or shift to the right:

Decreased Temperature

A

Shift to the left

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18
Q

Shift to the left or shift to the right:

increased Organic phosphates

A

shift to the right

19
Q

Shift to the left or shift to the right:

Increased p(CO2)

A

Shift to the right

20
Q

Shift to the left or shift to the right:

decreased p(CO)

A

Shift to the right

21
Q

Shift to the left or shift to the right:

increased pH

A

Shift to the left

22
Q

it decreases oxygen affinity, more 02 release to the tissues

A

Right shift

23
Q

Increase oxygen affinity, less 02 release to the tissues

A

left shift

24
Q

Hemoglobin in combination with oxygen, it gives pinkness to the skin and mucous membrane and seen in arterial circulation

A

Oxyhemoglobin

25
Q

Hgb with iron but no O2 seen in venous circulation/unassociated with oxygen

A

Deoxyhemoglobin

26
Q

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

A

Embryonic Hemoglobin

27
Q

Hemoglobin gower 1
Hemoglobin gower 2
hemoglobin portland

A

Composed of 2 zeta and 2 epsilon globin chains
Composed of 2 alpha and 2 epsilon
composed of 2 zeta and 2 gamma

28
Q

the major hemoglobin of the fetus and newborns
Composed 0f 2 alpha and 2 gamma
Produced four months after conception

A

Fetal Hemoglobin

29
Q

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)

A

Hemoglobin A or A1

30
Q

Constitutes less than 3% of the total hemoglobin
Composed of 2 alpha and 2 delta

A

Hemoglobin A2

31
Q

degradation product of HbA2
composed of 2 alpha and 2 delta

A

Hemoglobin A3

32
Q

This is the primary hemoglobin in people with sickle cell disease.
Those with Hb S disease have two abnormal beta (βS) chains and two normal alpha (α) chains.
causes the red blood cell to deform and assume a sickle shape when exposed to decreased amounts of oxygen.

A

Hemoglobin S

33
Q

is replaced by valine in the 6th position of beta chain

A

Glutamic Acid

34
Q

About 2-3% of people of West African descent are heterozygotes for this hemoglobin (have one copy of βC).
This hgb disease (seen in homozygotes
– those with two copies of βC).
instead of glutamic acid , lysine is in B6
It usually causes a minor amount of hemolytic anemia and a mild to moderate enlargement of the spleen.

A

Hemoglobin C:

35
Q

Hemoglobin E is one of the most common beta chain hemoglobin variants in the world.
People who are homozygous for Hb E (have two copies of βE) generally have a mild hemolytic anemia, microcytic red blood cells, and a mild enlargement of the spleen.
A single copy of the hemoglobin E gene does not cause symptoms unless it is combined with another mutation, such as the one for beta thalassemia trait.

A

Hemoglobin E:

36
Q

an abnormal hemoglobin that occurs in some cases of alpha thalassemia .

It is composed of four beta (β) globin chains and is produced in response to a severe shortage of alpha (α) chains.
A

Hemoglobin H:

37
Q

Are acquired hemoglobin variants whose structure has been modified by drugs or environmental chemicals.
do not transport oxygen to the tissue well resulting in
cyanosis.

A

methemoglobin
sulfhemoglobin
Carboxyhemoglobin

38
Q

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.
Causes :
Presence of oxidants
Genetic deficiency – decrease activity of MethHB

A

METHEMOGLOBIN ( HI)

39
Q

Formed by the irreversible oxidation of Hb of certain drugs and chemicals.
examples :
sulfonomides
phenacetin
acetanilide
Formed by the addition of hydrogen sulfide to Hgb has a
greenish pigment.
If it reaches the critical level in the blood it imparts MAUVE LAVENDER

A

SULFHEMOGLOBIN

40
Q

In condition known as enterogenous cyanosis

A

Sulfhemoglobin

41
Q

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.
Carbon monoxide is termed as silent killer for its colorless gas , odor and patient becomes easily hypoxic.

A

CARBOXYHEMOGLOBIN

42
Q

qualitative screening test based on specific gravity. the density of the drop of blood is directly proportional to the amount of the hemoglobin it contains.

A
  1. Copper Sulfate Specific Gravity -
43
Q

principle of the copper sulfate sg test

A

when the drop of donor`s blood dropped into copper sulfate solution comes incased in a sac of copper proteinate, which prevents any change in the sg for abt. 15 sec

HEMA LEC (3 decks)

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