None of the above

Corrected by adding 0.1g of potassium carbonate to the cyanmethemoglobin reagent

Corrected by making a 1:2 dilution with distilled water (1 part diluted specimen plus 1 part water) and multiplying the results from the standard curve by 2

corrected by adding 0.01 mL of the patient’s plasma to 5mL of the cyanmethemoglobin reagent. Using this solution as the reagent blank.

Store in a brown bottle or in a dark place

Plasma Na+

Intracellular Na+

Plasma K+

Intracellular K+

Acid Hematin Method

Direct Matching Methods

Alkali Hematin Method

Method of Wong

Oxyhemoglobin Method

In this method, blood is mixed with a dilute solution of either sodium carbonate or ammonium hydroxide. The depth of the resulting color is then measured in a photoelectric colorimeter.

The advantage of this method is that it is accurate because carboxyhemoglobin and sulphemoglobin are converted to alkali hematin as well.

The disadvantage is that it will not accurately measure the hemoglobin of an adult.

The hemoglobin is converted to a yellow-colored solution of alkali hematin.

None of the statements are true.

Abnormal globulins, such as those found in plasma cell myeloma or Waldenstrom macroglobulinemia, may precipitate in the reagent; however this is corrected by adding 0.1g of potassium carbonate to the cyanmethemoglobin reagent.

A high WBC count (greater than 20 x 10^9/L) or a high platelet count (greater than 700 x 10^9/L) can cause turbidity and a false low result

The ferricyanide converts the hemoglobin iron from the ferric state to the ferrous state to form methemoglobin which then combines with K cyanide to form the stable pigment cyanmethemoglobin.

The color and intensity are measured spectrophotometrically at 400 nm.

Its advantage is that all forms of hemoglobin are measured.

Shortens the maturation time of developing erythroid precursors

Transforms the CFU-E into the earliest recognizable RBC precursor

Decreases stimulation of erythropoiesis when cellular hypoxia increases

Increases the rate of red blood cell production by the bone marrow

Normally, 1 to 2 mg of iron per day is lost by shedding of epithelial cells of GI tract, skin epithelial cells and renal tubules.

As body stores decrease, the absorption of iron falls.

Iron balance is regulated by several conditions namely: the amount of iron ingested, the amount of iron absorbed, red blood cell formation using recycled and new iron, iron stores and lastly iron loss through blood loss or other sources.

There is no physiological regulated mechanism for iron excretion.

Iron balance is mainly achieved by regulating the absorption of iron in the diet.

Increase in pH

Increase in carbon dioxide

Increase in temperature

Increase in 2,3-DPG

All conditions mentioned above cause a shift to the right.

Circulate longer than usual before reaching maturity

Show diffuse basophilia with Wright's stain

May be termed shift or stress reticulocytes

Loss of residual RNA occurs immediately upon marrow release

Ferritin

Hemosiderin

Transferrin

Myoglobin

Hemoglobin

The heme portion involves four iron atoms in the ferric state surrounded by protoporphyrin IX, or the porphyrin ring.

The globin portion consists of carbohydrates linked together. The heme and globin portions of the hemoglobin molecule are linked together by chemical bonds

 2,3- DPG combines with the alpha chains of deoxyhemoglobin and diminishes the molecule’s affinity for oxygen

All of the above

None of the above

Mechanical hemolysis

Occurs within the lumen of blood vessels

Fragmentation of RBC

Acidic pH

Release of these cells to the circulation has long-term effectivity in correcting anemia

Reticulocytes that are shifted from the bone marrow later than normal

Eosinophic cytoplasm which is responsible for its characteristic polychromasia

Very basophilic because they have not spent as much time degrading their ribosomes or making hemoglobin as they normally would before entering the bloodstream

Basophilic normoblast

Pronormoblast

Orthochromic normoblast

Polychromatophilic normoblast

95% of the colour develop at the end of 20 minutes. 98% of the color develop at the end of 30 minutes. The maximum color is reached after about 2 hours

The colored solution is then measured colorimetrically by comparing with a standard

Hydrochloric acid does not convert all forms of hemoglobins

Sources of error in this method include: visual error, technical errors and errors inherent in the equipment

In this method, hemoglobin in the blood is converted to acid hematin, a brown colored solution formed upon the addition of 1/10 N Hydrochloric Aci

Hepcidin is synthesized in the spleen

Hepcidin is the central regulator of iron homeostasis and it controls absorption and storage

Hepcidin catalyzes iron transfer from the enterocyte to plasma by binding to ferroportin

When hepcidin levels fall, iron gets stored within enterocytes forming mucosal ferritin and is shed with the cells

All of the above

Hemoglobin has the capacity to combine with carbon monoxide in the same proportion as with oxygen, but the affinity of the hemoglobin molecule for carbon monoxide is 20 times greater

Increased affinity results in the binding of carbon monoxide to hemoglobin to form carboxyhemoglobin even if the concentration of carbon monoxide is extremely low

The molecule forms an extremely unstable compound, which renders the hemoglobin molecule useless for oxygen transport. Carboxyhemoglobin displaces oxygen and leads to tissue hypoxia

All of the above

None of the above

Heme synthesis occurs in most body cells especially in the mature erythrocytes

Heme synthesis begins in the cytoplasm with the condensation of succinyl-CoA and glycine to form 5-aminolevulinic acid

The most important limiting step in this reaction is the rate of conversion to delta-ALA, which is catalyzed by the enzyme ALA synthetase

Two molecules of PBG condense into a cyclic tetrapyrrole to form uroporphyrinogen I or III

ll of the above

Stomach

Colon

Ileum

Duodenum

Kidney

Extravascular Hemolysis

Testosterone

Hypoxia

Pituitary Hormone

10days

60 days

120days

1day

To detect the oxygen carrying capacity of blood

To assist in detecting disease which cause a deficeincy or excess of hemoglobin  

To calculate red cell indices and check haemoglobin level prior to donating blood

To detect anemia and its severity 

All of the above

yolk sac

kidney

liver

bone marrow

spleen

A. Iron is classified as a trace element in the body since having increased levels of iron is toxic to our bodies.

B. Most of the iron is found in myoglobin

C. Moderate amounts are found in plasma

Only A and B

Only B and C

Iron is bound to protein and stored in the body in two forms. Two-thirds of the iron is stored as hemosiderin and one-third as ferritin.

Iron stores of women are generally higher compared to men.

Serum ferritin levels reflect the iron stores.

Hemosiderin is water-soluble and not visible by light microscopy.

All of the above

Termina Differentiation

Apoptosis

Necrosis

Cellular Senescence

In this method, hemoglobin will combine with and liberate a fixed quantity of oxygen. The blood is hemolyzed with saponin and the oxygen is collected and measured in a Van Slyke apparatus.

It has no advantage, but has several disadvantages like it is time consuming, uses expensive equipment and is inaccurate.

The volume of oxygen is corrected for temperature and pressure and the hemoglobin is determined by the following formula: mg. of iron per 100 ml/ 3.4 = grams of haemoglobin per 100 ml

The methods were formerly used to calibrate instruments for determining the Hb concentration.

All of the statements mentioned above are true

Most mutations that cause α -thalassemia are point mutations

In conditions of silent carrier state, there are two inactive genes.

In conditions of α -thalassemia trait, there are three inactive genes.

Fetuses with hydrops fetalis with Hb Bart are incompatible with life and therefore die in utero or shortly after birth.

All of the above

Spleen

Brain

Liver

Kidney

In men, a maximum of 30 ml of oxygen can be carried in combination w/ hemoglobin in each 100 ml of blood

In normal conditions, whole blood of men contains an average of 14 g of Hgb per 100 ml and for women, it contains an average of 15 g per Hgb 100 ml.

Red blood cells have the ability to concentrate hemoglobin in the cell fluid up to 50 grams in each 100 ml of cells

Each gram of hemoglobin can combine with 1.34 ml of oxygen if hemoglobin is 100% saturated.

In women, a maximum of 60 ml of oxygen can be carried in combination w/ hemoglobin in each 100 ml of blood

In vitro and in the presence of oxygen, hemoglobin reacts with hydrogen sulfide to form a greenish derivative called sulfhemoglobin.

Precipitation of hemoglobin as Heinz bodies occurs with further change.

The affinity of sulfhemoglobin for oxygen is 100 times lower than that of normal hemoglobin. It may be toxic at a very low level.

All of the above

None of the above

Basophilic normoblast

Polychromatophilic normoblast

Orthochromic normoblast

Pronormoblast

Erythroleukin Producing Factor

Interleukin-EPO

Erythropoietin Inducing Factor

Erythropoietin

Severe burns

polycythemia vera

High altitude

pregnancy

none of the above

Basophilia of the cytoplasm increases

Cell diameter increases

Nucleus to cytoplasm ratio (N:C) decreases

Nuclear chromatin becomes less condensed

Decrease pH

Decrease hydrogen ions

Decrease carbon dioxide

Decrease in 2,3-DPG

All conditions mentioned above cause a shift to the left.

Polychromatophilic erythrocyte

Pronormoblast

Prorubricyte

Orthochromatic rubricyte

Vegetarian’s dietary sources contains lower amounts of iron; however, vegetables are in the form of heme iron, so they are absorbed better

One of the factors that favor iron absorption is sugars in the diet.

Numerous factors inhibit iron absorption. Two of which are citric acid and hydrochloric acid of the stomach

Once absorbed, the iron molecule is converted from the ferrous to the ferric state by stomach acid.

Daily iron requirement for men is generally higher as compared to women

Iron deficiency related to lack of iron intake is seen in patients with tropical sprue- a chronic immune disorder that damages the small intestine and is triggered by eating foods containing gluten

Conditions related to lack of iron intake lead to iron deficiency. An example of these conditions is menorrhagia

Infants and children are susceptible to iron deficiency because of their growth spurts

Most cases of iron deficiency are indirectly related to external blood loss, especially menorrhagia or slow gastrointestinal bleed

Treatment for iron deficiency is aggressive therapeutic phlebotomy

Decreased serum iron 

Decreased percent saturation 

Decreased serum ferritin

Decreased total plasma iron binding capacity

None of the above 

Polychromatophilic erythrocyte

Basophilic normoblast

Orthochromic Normoblast

Metarubricyte

Only Dare’s procedure is accurate

The Direct Matching methods are sometimes used at the bedside of the patient by the physician

Drops of blood are allowed to fall into small bottles labeled with corresponding hemoglobin values.

One of the disadvantages of this method is that it is complex and inconvenient and takes too long to perform.

All of the above

The disadvantage of this method is that traces of copper present in the diluting fluid may convert hemoglobin to methemoglobin resulting in a false high result.

It is fast and accurate.

In this method, blood is added to dilute NaOH. The solution is boiled. The hemoglobin is converted to a blue green colored solution.

All of the above

none of the above

A. In cases of porphyria, patients may present with mild anemia and neurological changes.

B. Disorders in the synthesis of porphyrin or the heme moiety may be either inherited or acquired.

C. Lead poisoning leads to the inactivation of uroporphyrinogen III synthase.

Only A and B

Only A and C

Cords

Sinuses

Endosteum

Islands

Gower-1: 2 alpha and 2 zeta

Portland-1: 2 zeta and 2 gamma

Gower-2: 2 alpha and 2 epsilon

Hemoglobin F: 2 alpha and 2 gamma

Hemoglobin A: 2 alpha and 2 beta

Iron is recycled from heme and amino acids from globin of red cell senescence.

Once in the reticuloendothelial system, the ingested hemoglobin is broken down and heme is returned to the bone marrow, and the amino acids of the globin chain are returned to the amino acid pool.

Each of these products will later be recruited for hemoglobin formation and red cell production. In the adult, approximately 95% of recycled iron is used for red cell production.

All of the above

None of the above

Iron overload leads to the presence of iron deposits in the red cell precursors in the marrow called “sickle cells” as well as decreased serum ferritin

The disorders in this category are either inherited or acquired.

Primary iron overload may result from excessive dietary, medicinal, or transfusional iron intake or due to metabolic dysfunction.

Secondary iron overload is most frequently associated with hereditary hemochromatosis (HH)

Treatment for iron overload is given orally in the form of drops, which is good for infants and children, or tablets.

A value of 2% methemoglobin formed each day in our bodies is toxic

Aniline drugs and some antimalarial treatments may induce a methemoglobinemia in individuals who are unable to reduce methemoglobin.

Cyanosis develops if methemoglobin levels exceed 10%; hypoxia develops if levels exceed 60%.

All of the above

None of the above