Hemoglobin Flashcards
Most functional iron in humans
Hemoglobin
Myoglobin
Respiratory pigment
Hemoglobin
Storage form of iron
Ferritin
Hemosiderin
Iron that is incorporated into hemoglobin molecules
Heme
Reduced form of iron
Ferrous
Best time to take iron supplements
Early morning
Transport protein for iron
Transferrin
Main component of RBC
Hemoglobin
In 1RBC, what is the concentration of hemoglobin?
34g/dL
1g of Hb contains (iron)
3.47mg
Other term for heme
Protoporphyrin IX
Composition of heme
Carbon
Hydrogen
Nitrogen
With ferrous
Has four polypeptide chains and each chain is attached to 1heme group
Globin
Globin comprises how many amino acids?
141-146
Heme synthesis occurs in? In what stage?
Bone marrow
From Pronormoblast to reticulocyte
By products of heme synthesis
Delta aminolevulinic acid Porphobilinogen Uroporphyrinogen III Coproporphyrinogen III Protoporphyrinogen IX Protoporphyrin IX
Chromosome 16
Alpha and zeta
Chromosome 11
Beta, delta, gamma, epsilon
Production of globin chains take place in what stage
Pronormoblast to reticulocyte
Beta globin mRNA is translated more efficiently than?
Alpha globin mRNA
Oxygenated hemoglobin
Oxyhemoglobin
Oxyhemoglobin color? Seen in?
Arterial blood-bright red
Gower I
Zeta and epsilon
Portland
Zeta and gamma
Gower II
Alpha and epsilon
HbA
95% two alpha and two beta
HbA2
3-5% two alpha and two delta
HbF
1-2% two alpha and two gamma
HbF present in few RBC are called?
F cells
Formed by post synthetic, nonenzymatic reactions of various sugars with amino groups of the globin chain
HbA1
Normal adult hemoglobin
HbA
HbA2
HbF
Reference range
Male=14-18g/dL
Female=12-15g/dL
Newborn =16.5-21.5g/dL
Deoxygenated hemoglobin color? Seen in?
Venous blood-dark red
Hemoglobin with Carbon monoxide
Carboxyhemoglobin
Carboxyhemoglobin color?
Cherry red in blood and skin
Hemoglobin contains iron in the ferric state
Methemoglobin
Exposure to oxidizing agent will result to production of?
Methemoglobin
Characteristic of methemoglobin in the blood
Chocolate brown color
Treatment of methemoglobin
Administration of ascorbic acid or methylene blue
Formed by the irreversible oxidation of Hb by certain drugs and chemical
Sulfhemoglobin
In vitro Sulfhemoglobin gives?
Greenish pigment
A key rate limiting step in heme synthesis is suppression of
Aminolevulinate synthase
Ferric oxidation product of heme
Hemin
Amount of oxygen needed to saturate 50% of hemoglobin
P50 value
Curve
Sigmoidal
How many oxygen is bound by each gram of hemoglobin
1.34mL
Shifts of the curve to the left or right occur if there are changes in the pH of the blood
Bohr effect
Normal PO2
27mm hg
Shifts to the left
Higher oxygen affinity
Lower release of oxygen
Shift to the right
Lower oxygen affinity
Higher release of oxygen
Its oxygen affinity is 240times and 10000 times slower oxygen release
Carboxyhemoglobin
Increase 2,3-BPG
Shift to the right.
Decrease oxygen affinity
Lower pH or increase in Hydrogen concentration
Shift to the right
Decrease oxygen affinity
Decrease PCO2
Shift to the left
Increase oxygen affinity
Increase in temperature
Shift to the right
Decrease oxygen affinity
Presence of methemoglobin and Sulfhemoglobin
Shift to the left
Increase oxygen affinity
Amount of oxygen in 1g of hemoglobin
1.34mL
Amount of oxygen in 1g of hemoglobin
1.34mL