Hematology Midterm 2.0

C

Hemoglobin

Is the single most common complex organic molecule in the vertebrae.

hemolysis

Hemoglobin are generated from the RBCs thru ___________ and has a short half-life outside the RBC

34 g/dL

Concentration of Hb in RBC

64 thousand daltons

Molecular Weight of Hb

ribosomes

The globin portion of hemoglobin is produced on specific____________ in the cytoplasm of the red blood cells

Polypeptide chains

It is made up of amino acids that synthesized in the ribosomes

alpha, beta gamma, delta, epsilon, zeta

6 types of Globin chains

alpha

Globin chain that has 141 no. of amino acids

39

Gamma differs from Beta chain by ____ amino acids

Alanine

The 136th amino acid of Gamma A stands for _______.

Glycine

The 136th amino acids of Gamma G stands for ______.

Protoporphyrin IX

Nitrogenous substance and synthesized partly inside the mitochondria and partly in the cytoplasm of a nucleated RBC.

Mitochondria

Heme is synthesized in the _____________.

Ferrous iron

Incorporate with the center of protoporphyrin IX thus forms ferroprotoporphyrin IX or heme

3.47 mg

1 gram of hemoglobin is equal to _____________ of Ferrous iron

2,3-diphosphoglycerate

It is produced in Rapoport pathway

decreases

When hemoglobin binds (2,3-DPG/BPG) oxygen affinity ______________

increases

when the plasma level of 2,3-DPG decreases, Hb 2,3-DPG is released, the Hb affinity for O2 ___________.

Hemoglobinopathy

Qualitative/structural defects due to amino acid substitution.

Thalassemia

Quantitative / synthetic due to deletion or addition of amino acids

3

How many dimension is the hemoglobin?

globular

Shape of hemoglobin

4

How many globin chains are there in a hemoglobin?

1

How many 2,3 DPG in a hemeglobin?

4

How many heme groups are there in a hemoglobin?

a and b bonds

What are the bonds that connect globin chains?

a bonds

Connects 1 alpha and 1 beta chains

b bonds

Connects dimers allow two dimers to move relative to each other.

Tense form

non-oxygenated form of Hb

Relaxed form

oxygenated form of hemoglobin

Tense form

Forms anionic bridges between beta chains and they move farther from each other

Relaxed form

Partial oxygenation of 2,3-DPG is expelled and permits further oxygen binding.
Salt bridges are broken and they move together

non-conjugating

Globin chains are simple __________proteins consisting of amino acids only

peptide bonds

The amino acids are connected by the___________ in a specific sequence to form a given globin chain.

11,16

The genes along chromosomes ____and ____ each provide a unique DNA code for each globin type.

Primary Structure

Specified sequence of amino acid residues that together form a certain types of globin chain

N-terminal

Beginning of amino acid chain

C-terminal

End of the amino acid chain

8

There are how many helical segments in a secondary structure?

Secondary structure

This structure provide the flexibility that allows physical bending of the globin chain to form tertiary structure

Tertiary structure

These are bending of hemoglobin
Arrangement of helices into a 3-dimensional, pretzel like structure.

Quaternary Structure

Complete molecule which is spherical

nucleus

Transcription of globin chains to messenger RNA occurs in the_________

ribosomes

Translation of mRNA to the globin polypeptide chain occurs in the __________ in the cytoplasm

heme

It consists of ring of carbon, hydrogen, and nitrogen atoms called protoporphyrin IX, with a central atom of divalent ferrous iron.

Methemoglobin

Are the Oxidized hemoglobin

Fe3

Ferric State

Fe2

Ferrous state

mitochondria and cytoplasm of bone marrow erythrocyte precursors

Heme biosynthesis occurs in the _______________________________, beginning with the pronormoblast through the circulating polychromatic erythrocyte.

Iron

_____in the ferrous state is required to convert protoporphyrin to heme.

Ferritin

Storage form of iron

hemosiderin

If apoferritin is unavailable, iron is stored in _________.

small intestine

90% iron goes to __________

10

Only ____% of iron is absorbed

Ferrous state

Is the only one who is absorbed then the ferric state is not absorbed

stomach

Reduction of ferric to ferrous state of iron occurs in ___________.

stomach and small intestine

Absorption of iron takes place in ___________.

endosome

Acidification of the ____________ releases the iron from transferrin

ferro chelatase

The insertion of ferrous iron into the center of the protoporphyrin IX molecule is aided by the enzyme ____________.

17,000 daltons

Myoglobin has a molecular weight of _____________

Myoglobin

________ is a heme pigment found in striated muscle

1

Myoglobin has ________ heme molecule attached to the polypeptide chain.

oxygen dissociation curve

A significant difference between myoglobin and hemoglobin is the _________________

hyperbolic

oxygen dissociation curve of myoglobin is ________

sigmoid

oxygen dissociation curve of hemoglobin is ________

12-16 g/dL

Hb Reference Range for Female

13.5-17.5 g/dL

Hb Reference Range for Male

14.5-22.5 g/dL

Hb Reference Range for Newborns

1

1 heme polypeptide unit of Hb molecule= ___________O2 molecule

1.34

1 g Hb= ____mL O2

y

The __-axis reflects to the percentage of hemoglobin saturation.

Curve B

It represents shift to the left decrease temperature decrease to 2-3 DPG and so forth.

Curve A

It represents shift to the right reduced affinity increase.

increases

Between 20 to 60 mmHg the affinity__________substantially.

Blood temperature, Erythrocyte 2,3-DPG, CO2, pH, Amount of Hb F, Abnormal hemoglobin variants

Factors Affecting hemoglobin Affinity for Oxygen

70, plasma bicarbonate

___% of CO2 is carried to the lungs in the form of __________

20

___% of CO2 is carried to the lungs in the form of erythrocyte bicarbonae

CO2 Dissociation Curve

Reflects the relation between blood CO2 content and the pCO2 for non-oxygenated blood and oxygenated blood

Haldane

CO2 Dissociation curve is known as ________effect

45

Angle for arterial blood gas

Hemoglobin deriivatives

_____________are abnormal forms in which heme is altered in some way but the globin chains are unaffected

Carboxyhemoglobin

Is a carbon monoxide derivative of your hemoglobin

200x

Hb affinity to CO is ______ greater than its affinity to O2

Brilliant, cherry red

Color of Carboxyhemoglobin

Defective Stoves, Illuminating Gas, Gas heaters, Gasoline motors, Smoking of tobacco

Chief sources of carboxyhemoglobin

F

T or F: Heme can bind oxygen in carboxyhemoglobin and methemoglobin.

Methemoglobin

Is formed by oxidation of iron to ferric state

Methemoglobinemia, cyanosis

This results in inability to adequately reduced methemoglobin that builds up in the circulating therefore causing _________

Cyanosis

Bluish discoloration of the skin due to reduced oxygenation of the blood

diaphorase deficiency

In Inherited Methemoglobinemia there is NABH methemoglobin reductase enzyme deficiency also called ___________________.

anti-malarial drugs, sulfunamides

Where can Methemoglobinemia acquired?

Sulfhemoglobin

Hemoglobin oxidation by certain drugs and chemicals in vivo

enterogenous cyanosis

Sulfhemoglobin is Reported in patients with severe constipation, in cases of bacteremia due to Clostridium perfringens and in condition known as ____________________.

Cyanmethemoglobin, Oxyhemoglobin, Harboe, Naumann Method

What are the laboratory method of evaluating hemoglobin

Cyanmethemoglobin Method

Measurement of total Hb in whole blood

sulfhemoglobin

Cyanmethemoglobin measures in all forms of peripheral blood hemoglobin except _______________

Drabkin's solution, 540 nm

Solution used in Cyanmethemoglobin method and yje color intensity

Oxyhemoglobin Method

Measure plasma hemoglobin for diagnosis of acute hemolytic episodes

Harboe Method

Plasma Hb is measured as oxyhemoglobin at 415 nm.

Naumann Method

Uses benzidine derivatives in which Hb catalyzes the rapid oxidation of benzidine by hydrogen peroxide.