Hemoglobin Flashcards
how many ml of oxygen can a One gram of Hgb can carry?
1.34ml
Function of the Hgb.
•Transport oxygen from the lungs
to the tissue and carbon dioxide
from the tissue.
•Acid –base balance regulation
Hemoglobin H
Abnormal hemoglobin occur in some case of alpha thalassemia. Composed of 4 beta globin chain produced in response to severe shortage of alpha chain
One of most common beta chain hemoglobin variant in the world. People who have homozygous for Hb E have 2 copies of (beta epsilon) generally have mild hemolytic anemia, microcytic red blood cells and large enlargement of spleen. Single copy of hemoglobin E does not cause symptoms unless it is combined with another mutation, such as 1 for beta thalassemia trait.
Hemoglobin E (Egal)
Temperature shift to the left
Decrease
pH shift to the right
Decrease
Organic phosphate shift to the left
Decrease
Number of amino acid- 141
Alpha and Zeta
Number of Amino Acid- 146
Beta, Gamma A, Gamma B, Delta, Epsilon
Results from binding of carbon monoxide to heme iron. Hb can combine with carbon monoxide with affinity 200 times greater than Oxygen.
Carbon monoxide termed as silent killer for its colorless gas, odor and patient becomes easily hypoxic.
Carboxyhemoglobin
Affinity of 200-240 time greater than Oxygen
Carboxyhemoglobin
Treatment= Intravenous methylene blue- %
Methemoglobin
Binding and releasing of hemoglobin to oxygen, oxygen to pH
Affinity
(SgaVal) primary hemoglobin in people with sickle cell disease. Those with Hb S disease have 2 abnormal beta chain and 2 normal alpha chain.
Cause of red blood cell to deform and assume sickle shape when expose to decrease amount of oxygen.
Hemoglobin S
is replaced by valine in the 6th position of beta chain
Glutamic acid
(FAG) major hemoglobin of fetus and newborns. Compose of 2 alpha 2 gamma. Produce 4 months after conception.
Fetal hemoglobin
Synthesis of globin
occurs in ribosomes using messenger RNA that is translated into polypeptide chain. Synthesis of globin is controlled in the chromosomes of alpha and beta.
Normal adult hemoglobin. 95 to 97% of hemoglobin in normal adults produced after 1 year onwards. Composed of 2 alpha (141 AA) and 2 beta chain (146 AA)
Hemoglobin A or A1
1 heme
1 mole of oxygen
1 hbg
4 moles of oxygen
1 gram of hemoglobin
Carry 1.34 of oxygen
Heme synthesis
Produce complete heme, 8 steps involved 4 enzymes in mitochondria and 4 enzyme in cytoplasm
Heme
Occurs in mitochondria and cytoplasm of bone marrow
Sulfhemoglobin
Form by irreversible oxidation of Hb of certain drugs and chemical.
A. Sulfonamides
B. Phenacitin
C. Acetinalde
Form by addition of hydrogen sulfide to hgb has a greenish pigment.
If sulfhemoglobin reaches critical level in blood it imparts mauve lavender.