Hemoglobin

Question 1

to An iron bearing protein contained within the erythrocytes

Answer 1

Hemoglobin

Question 2

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

Answer 2

young erythroblast & polychromatophilic normoblast

Question 3

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

Answer 3

1.34 ml

Question 4

what are the composition of heme?

Answer 4

Protophorphyrin IX, Ferrous iron

Question 5

What compose the 4 globin structure

Answer 5

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

each globin - 8 helices separated by 7 non helices segments

Question 6

number of amino acids of Alpha & Zeta

Answer 6

141

Question 7

Complete hemoglobin molecule described by?

Answer 7

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

Question 8

Occurs in the cytoplasm of normoblast and reticulocytes

Answer 8

Globin

Question 9

It is manufactured in the ribosomes

Answer 9

polypeptide chains

Question 10

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

Answer 10

Globin protein

Question 11

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

Answer 11

true

Question 12

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

Answer 12

Nitric oxide

Question 13

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

Answer 13

Oxygen Affinity

Question 14

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

Answer 14

true

Question 15

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

Answer 15

Bohr effect

Question 16

Modified true or false :

Inc pH ( alkalosis)= dec Hb affinity for O2

Dec pH ( acidosis )= inc hb affinity for O2

Answer 16

both false

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

Question 17

Shift to the left or shift to the right:

Decreased Temperature

Answer 17

Shift to the left

Question 18

Shift to the left or shift to the right:

increased Organic phosphates

Answer 18

shift to the right

Question 19

Shift to the left or shift to the right:

Increased p(CO2)

Answer 19

Shift to the right

Question 20

Shift to the left or shift to the right:

decreased p(CO)

Answer 20

Shift to the right

Question 21

Shift to the left or shift to the right:

increased pH

Answer 21

Shift to the left

Question 22

it decreases oxygen affinity, more 02 release to the tissues

Answer 22

Right shift

Question 23

Increase oxygen affinity, less 02 release to the tissues

Answer 23

left shift

Question 24

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

Answer 24

Oxyhemoglobin

Question 25

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

Answer 25

Deoxyhemoglobin

Question 26

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

Answer 26

Embryonic Hemoglobin

Question 27

Hemoglobin gower 1 Hemoglobin gower 2 hemoglobin portland

Answer 27

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

Question 28

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

Answer 28

Fetal Hemoglobin

Question 29

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)

Answer 29

Hemoglobin A or A1

Question 30

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

Answer 30

Hemoglobin A2

Question 31

degradation product of HbA2 composed of 2 alpha and 2 delta

Answer 31

Hemoglobin A3

Question 32

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.

Answer 32

Hemoglobin S

Question 33

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

Answer 33

Glutamic Acid

Question 34

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.

Answer 34

Hemoglobin C:

Question 35

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.

Answer 35

Hemoglobin E:

Question 36

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.

Answer 36

Hemoglobin H:

Question 37

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.

Answer 37

methemoglobin sulfhemoglobin Carboxyhemoglobin

Question 38

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

Answer 38

METHEMOGLOBIN ( HI)

Question 39

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

Answer 39

SULFHEMOGLOBIN

Question 40

In condition known as enterogenous cyanosis

Answer 40

Sulfhemoglobin

Question 41

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.

Answer 41

CARBOXYHEMOGLOBIN

Question 42

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.

Answer 42

1. Copper Sulfate Specific Gravity -

Question 43

principle of the copper sulfate sg test

Answer 43

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