Hemoglobin, Hematocrit, ESR Determination, RBC indices Part 1

Hemoglobin

is a respiratory pigment because its primary function in the body is respiratory function.

Respiratory function

Primary function of hemoglobin in the body

Hemoglobin

is responsible for the carrying of oxygen from the lungs which will be delivered to the tissues.

Carbon dioxide

After the oxygen has been effectively delivered to the tissues, the hemoglobin will also carry waste products of catabolism from the tissues.

What is this waste product of catabolism?

detrimental effects

Since carbon dioxide is a waste product, it should be excreted out from the body because it causes __________________ to any patient's condition if left accumulated inside the body.

lungs

Once the hemoglobin molecule effectively delivers the oxygen to the tissues, the carbon dioxide will be transported to the ______ for excretion (there is oxygen to carbon dioxide exchange).

Hemoglobin

is responsible for the red color of the blood.

Heme, Globin

The hemoglobin molecule is composed of:

Heme

Iron portion of hemoglobin

Globin

Protein component of hemoglobin

Heme

The specific component of hemoglobin molecule that is responsible for the red color of the blood.

Ferrous or reduced

Heme has to be maintained in its _______ state all the time in order for the hemoglobin molecule to be fully functional and to perform its respiratory function in the body.

Fe2+

Chemical notation for Ferrous iron

Conjugated protein

What kind of protein is hemoglobin?

Hemoglobin

is a conjugated protein whose primary function is to deliver O2 from the lungs to the tissues and to transport CO2 away to the lungs (respiratory function of blood)

Globin

The entire molecule of hemoglobin is composed of a protein component called?

Conjugated proteins

These proteins are soluble in plasma. It can mix in the plasma without being destroyed in the plasma.

Unconjugated proteins

These proteins are insoluble in plasma. These substances are destroyed once they go out to the plasma because they are not compatible with the environment in the plasma.

Always

How often is hemoglobin found inside the RBC?

very small type of protein molecule

Hemoglobin molecule is different from the usual proteins (which are big molecules) because hemoglobin is a?

High molecular weight

Proteins are molecules with what molecular weight?

Kidney

What organ filters the blood?

Glomerulus

What specific part of the kidneys selectively filter the blood?

Glomerulus

This specific part of the kidney only selects safe substances for it to pass trough its filtration.

High molecular weight

What molecular weight substances won't be filtered by the glomerulus of the kidneys because it will cause kidney damage?

Hemolytic episodes

when the RBCs are abnormally destroyed in the body due to a condition that provokes the abnormal destruction of the RBC

whatever hemoglobin molecule that destroyed RBC is protecting will eventually leak out to the plasma.

Hemoglobin

This molecule is a small type of protein, it can easily pass through the filtration rate of the glomerulus. Also, since it is high in molecular weight, constant filtration of this molecule in the glomerulus of the kidney will eventually damage the kidneys of the patient.

True

(True/False) Hemoglobin is compatible with the plasma environment because it is a conjugated protein.

False

(True/False) Hemoglobin is incompatible with the plasma environment because it is a unconjugated protein.

Haptoglobin, hemopexin, albumin

Body defense mechanisms that neutralize the liberated hemoglobin from the RBC

Haptoglobin

It is considered as the first line of defense against liberated hemoglobin

Haptoglobin

A normal, large, protein found in the plasma; transport protein of the hemoglobin molecule.

It is a conjugated protein and never filtered by the glomerulus of the kidneys.

Haptoglobin

This is the first to immediately bind to the liberated hemoglobin

Haptoglobin-Hemoglobin Complex

What is the complex formed when haptoglobin binds with hemoglobin?

1:1

Haptoglobin to hemoglobin ratio in the haptoglobin-hemoglobin complex

1

How many hemoglobin molecules can 1 haptoglobin molecule neutralize?

Liver

Once the haptoglobin-hemoglobin complex is formed, the entire complex will be transported to this organ and degraded.

Irreversible

The degradation of the haptoglobin-hemoglobin complex in the liver is (revserible/irreversible)

Irreversible

Degradation wherein the entire complex is degraded and destroyed permanently

Severely decreased or zero

Haptoglobin levels indicative of hemolytic episodes.

Hemopexin

It is considered as the second line of defense against liberated hemoglobin

Hemopexin

Transport protein of heme normally found in plasma as macromolecules

Heme, Globin

In pronounced hemolysis, when the levels of haptoglobin in the plasma are not enough to neutralize the increasing number of hemoglobin molecule that goes out to the plasma, eventually the hemoglobin molecule will split off into _______ and _________.

Globin

When there is not enough haptoglobin, hemoglobin breaks off into heme and globin. Which portion of the hemoglobin molecule is reused by the body for the synthesis of another hemoglobin molecule?

Heme

When there is not enough haptoglobin, hemoglobin breaks off into heme and globin. Which portion is the dangerous portion if it goes into the circulation?

Iron

This portion of the heme molecule is toxic to the plasma

Iron toxicity

If heme accumulates in the plasma, what condition can the patient get?

Hemopexin

When heme is released from the hemoglobin molecule, this molecule will immediately bind to it.

Hemopexin-Heme Complex

What complex is formed when hemopexin immediately binds to the liberated heme molecule?

Hemopexin-Heme Complex

This large complex cannot pass through the filtrate rate of the glomerulus of the kidneys.

Liver

What organ will the Hemopexin-Heme Complex be transported to?

Reversible

The degradation of the hemopexin-heme complex in the liver is (reversible/irreversible).

Heme

What portion of the Hemopexin-Heme Complex is degraded in the liver?

Hemopexin

What portion of the Hemopexin-Heme Complex is not degraded in the liver and goes back into the plasma and wait for another heme molecule to be neutralized.

Hemopexin

Since the Hemopexin-Heme Complex degradation is reversible (except for the Heme part), this molecule's levels in the plasma should not be used to indicate hemolysis or hemolytic episodes.

Hemopexin

This molecule doesn't get exhausted unless there is too much heme in the plasma.

longer

The time for the hemopexin to transport the entire complex to the liver is ________________, because the number of heme that accumulates in the plasma is too many.

Albumin

This is considered as the third line of defense for liberated hemoglobin

Albumin

This macromolecule is normally found in the plasma. This molecule attaches to the remaining heme in the plasma and forms another compound called methemalbumin.

Methemalbumin

This is the compound formed when albumin binds to the remaining heme molecules in the blood.

Fairley's pigment

Other name for methemalbumin

Kidney

Since albumin is another macromolecule type of protein, whatever heme that is already attached to the albumin can no longer pass through the filtrate rate of the ___________.

detach

Eventually, the albumin will _________ from the heme portion once the hemopexin in the plasma gets replenished after it delivers the hemopexin-heme complex for reversible degradation in the liver to happen.

temporary

The attachment of the albumin to heme is (permanent/temporary), and the same goes with the formation of methemalbumin

Schumm test

A laboratory test that determines the presence of methemalbumin in the patient's blood

Schumm test

This test differentiates intravascular hemolysis from extravascular hemolysis.

Intravascular hemolysis

Hemolysis inside the blood vessel

Extravascular hemolysis

Hemolysis outside the blood vessel

Brown discoloration

Positive results for Schumm test

Methemalbumin is present in the blood, intravascular hemolysis

Brown discoloration meaning for Schumm test

Intravascular

Of what origin is the hemolysis if the result of the Schumm test is a brown discoloration?

Kidneys

The main objective of the 3 different defense mechanism of the body (haptoglobin, hemopexin, albumin) is to protect what organ from being damaged when there is hemolytic episodes?

Hemoglobin

The oxygen- and carbon dioxide-carrying capacity of the red blood cell is attributed to this molecule.

directly proportional

The oxygen carrying capacity of the blood is (directly/indirectly proportional) to the hemoglobin content and not RBC count.

4 globin, 4 protoporphyrin IX, 4 iron, 1 2,3-DPG

What is the composition of a hemoglobin molecule?

Globin

The protein content of the hemoglobin molecule that contains 4 polypeptide chains

4

How many polypeptide chains does the globin portion have?

2

How many pairs of polypeptide chains are there in Globin?

2 alpha and 2 beta chains

What are the two polypeptide chains in a Globin molecule?

alpha polypeptide chain

This chain of globin contains 141 amino acids. Total of 282 because it is in pairs

beta polypeptide chain

This chain of globin contains 146 amino acids. Total of 292 because it is in pairs

141

How many amino acids are there in an alpha polypeptide chain?

282

How many amino acids are there in a pair of alpha polypeptide chains?

146

How many amino acids are there in an beta polypeptide chain?

292

How many amino acids are there in a pair of beta polypeptide chains?

146

How many amino acids in a gamma (γ) chain?

146

How many amino acids in a delta (δ) chain?

146

How many amino acids in an epsilon (ε) chain?

146

How many amino acids in a zeta (ζ) chain?

delta chain

This chain is differentiated from the beta chain in the 10th amino acid sequence. The 10th amino acid should not be the same in beta.

10th

The delta chain is differentiated from the beta chain in which amino acid sequence?

gamma chain

This chain is differentiated from the beta chain in the 39th amino acid sequence.

39th

The gamma chain is differentiated from the beta chain in which amino acid sequence?

epsilon and zeta chain

These chains are found in the embryonic life

Portland, Gower I, Gower II

Embryonic hemoglobins

4

How many molecules of Protoporphyrin is in hemoglobin?

Protoporphyrin IX

This is the nitrogenous substance in the hemoglobin molecule; has 4 molecules.

Protoporphyrin IX

This is synthesized partly in the cytoplasm of the nucleated RBC during maturation and partly inside the mitochondria of the nucleated RBC.

cytoplasm and mitochondria

Protoporphyrin IX is synthesized in the _?_ of the nucleated RBC during maturation

4

How many iron atoms are there in a hemoglobin molecule?