HEMA (Hemoglobin)

sequence and number of amino acids in chains

The difference in the globin chain relates both to the?

2a, 2e; embryonic

Molecular Structure and stage of life of Gower 2

2z, 2g; embryonic

Molecular Structure and stage of life of Portland

2a, 2g; newborn and adult

Molecular Structure and stage of life of Fetal Hb

2a, 2d; newborn and adult

Molecular Structure and stage of life of Hb A2

Mitochondria and cytoplasm of bone marrow erythrocyte precursors

Heme synthesis is synthesized in what organelles?

Uroporphyrinogen III cosynthetase

IN heme sythesis:

This enzyme is responsible to form uroporphyrinogen III

Uroporphyrinogen decarboxylase

IN heme sythesis:

This enzyme is responsible to remove a carbon to form coproporphyrinogen III

Rapoport-Luebering shunt

This is where 2,3 - Diphosphoglycerate is produced

Intravasculat hemolysis (10%)

Occurs when hb breaks down in the blood and free hb is released into plasma

haptoglobin, hemopexin and albumin and engulfed by macrophages

In intravascular hemolysis, Free hb will bind to?

Globin, Heme, Iron, protoporphyrin ring

In extravascular hemolysis Hg can be degraded into:

amino acid pool

When Hb is degraded into globin, amino acids will go back to?

ferritin

Storage area for iron in liver/spleen.

heme oxygenase

Enzyme that breaks down the alpha methene bridge of proptoporphyrin ring

zeta chain

epsilon chain

Embryonic Hb

analogue of a-chain

counterpart of the y, B and delta chain

Alkali Denaturation - HbF is not denatured

Kleihauer- Betke Acid Elution - HbF resists acid elution

HbF can be measured by and what is their results

FALSE

smaller

TRUE OR FALSE

After birth, large amounts of HbF are produced

97%

1.5% - 3.5%

Amount of HbA1 in normal adult

HbA2 amount of in normal adult

b-Thalassemias, hyperthyroidism, megaloblastic anemia

HbA2 is increased in what diseases?

Oxyhemoglobin (HbO2)

scarlet red/bright red color

Formed when the RBCs pass through the alveolar capillaries of the lungs

Color: ?

Carboxyhemoglobin (HbCO)

Color: Cherry Red

Chief Sources of CO: automobile exhaust, industrial wastes, tobacco smoking (10%)

Endogenous source: < 1%

Critical Value: 5g/100 ml

Treatment: administration of O2

Absorption wavelength: 576 nm

Oxygen molecules bound to heme are replaced by carbon monoxide.

Second most dangerous

Color: ?

Chief Sources of CO: ?

Endogenous source: ?

Critical Value: ?

Treatment: ?

Absorption wavelength: ?

Composition: 1 ml blood + 50 ml water

+: Cherry red - pink or bluish red: НьСО (carbon monoxide poisoning)

-: Yellowish red: НЬ02

Rapid test for HbCO

Dilution Test

Composition:

Positive reaction:

Negative reaction:

Composition: 1% Tannic acid

+: red ppt

-: Black brown discoloration: HbO2

Rapid test for HbCO

Tannic Acid Test

Composition:

Positive reaction:

Negative reaction:

Methemoglobin/Hemiglobin (Hi)

color: chocolate brown color of blood

daily: 0.5% - 3% hb → Hi

caused by: poisoning during oxidative drugs

absorption wavelength: 630 - 635 nm

Iron in the hemoglobin molecule is in the ferric (Fe3) state instead of the ferrous (Fe2) state.

Incapable of combining with oxygen

color: ?

daily: ?

caused by:

absorption wavelength: ?

Hemoglobin

64000 D

Makes up 35% of RBC

(It takes about the biggest part of RBC, volume, weight, color, size)

molecular weight: ?

Hg

The respiratory pigment of blood: gives the red color to the blood

1.34ml O2 and 3.47mg Fe

RATIO: 1 g = 1.34ml O2 and 3.47mg Fe

1 gm Hb can carry how many O2 and Fe?

Polychromatophilic normoblast

Stage where hemoglobin is completed

heme

What part of hemoglobin shows significance to iron?

True

TRUE OR FALSE

Hg represents > 1% of the total body weight and it occupies 28% of the red cell mass

Oxygen tension

Hb biosynthesis is regulated by what tension in the kidneys?

FALSE

Hg carries oxygen from higher oxygen tension to lower oxygen tension.

TRUE OR FALSE

Hg carries oxygen from lower oxygen tension to higher oxygen tension.

100 mm Hg

20 mm Hg

Lungs carry how many mm Hg of saturated oxygen?

How many mm Hg is carried to the tissues by Hb?

CO2

It is the waste product of ATP from red cells to lungs

carbaminohemoglobin

Hg with CO2 is called?

Globin chains, 4 Heme group, 2,3-Diphosphoglycerate

Components of Hb

Protoporphyrin IX + Fe+2

a Heme is composed of?

Protoporphyrin IX + Fe+3

A met Hb is composed of?

Ribosomes; basophilic normoblast and polychromatophilic normoblast

Globin chains are dimer synthesized in what organelle of what stage?

Globin chain

Determines the type of Hb

chromosome 16

chromosome 11

What chromosome is alpha chain produced?

What chromosome is beta chain produced?

2z, 2e; embryonic

Molecular Structure and stage of life of Gower 1

2a, 2b; newborn and adult

Molecular Structure and stage of life of Hb A1

Hb A1

Type of Human Hb that is prominent in adult

Hb A2

Type of Hb that acts as a back up

unknown

No. of amino acid for epsilon

141

No. of amino acid for zeta and alpha chain

146

No. of amino acid for beta, delta, gamma chain

TRUE

TRUE OR FALSE

Heme synthesis has trace amount in basophilic normoblast and its completion is seen in polychromatophilic normoblast

Protoporphyrin IX and iron (Fe+2)

Product of a broken down heme

Ferrochelatase

IN heme synthesis,

Protoporphyrin IX incorporates iron to the heme with the use of this enzyme

FALSE

high affinity

TRUE or FALSE

Hb has a normal affinity to oxygen

TRUE

TRUE or FALSE

2,3 - DPG is directly proportional to oxygen in tissue

FALSE

indirectly proportional

TRUE or FALSE

2,3 - DPG is directly proportional to Hb affinity

Salt bridges

2,3 - DPG forms this bridges to regulate Hb and O2 affinity

2,3 - DPG

Facilitate the unloading oxygen from Hb in the tissues

R form and T form

Two forms of 2,3-DPG when it is expanded

R form (relaxed form)

Form of 2,3-DPG

Hemoglobin has a higher affinity for oxygen, meaning it binds oxygen more readily.

Oxygen is bound to hemoglobin

T form (tensed form)

Form of 2,3-DPG

Hemoglobin has a lower affinity for oxygen, meaning it releases oxygen more readily.

Oxygen is not bound to hemoglobin

Lungs; High oxygen tension

In T form,

This is where salt bridges formed will dissolve, due to what tension?

diminished

less flexible

increases

IN RBC Destruction:

What will happen to enzyme activity especially in glycolysis during breakdown of RBC

What will happen to the membrane of RBC during its destruction?

What will happen to the concentration of cellular hemoglobin?

towards the end of 120 day life span

When will RBC begin to break down?

INCREASE

INCREASE OR DECREASE

In the laboratory, the effect of intravascular hemolysis to plasma Hb __

INCREASE

INCREASE OR DECREASE

In the laboratory, the effect of intravascular hemolysis to serum bilirubin __

INCREASE

INCREASE OR DECREASE

In the laboratory, the effect of intravascular hemolysis to serum LDH __

DECREASE

INCREASE OR DECREASE

In the laboratory, the effect of intravascular hemolysis to serum haptoglobin __

extravascular

90% of hemolysis happens?

degraded into biliverdin

When Hb is degraded into heme, what will happen to protoporphyrin?

will be recycled into circulation

When Hb is degraded into heme, what will happen to Fe?

B-1-globulin

When Hb is degraded into iron and split off, what will remove its attachment?

Transferrin

If iron is reused, what will be its carrier protein?

hemosiderin

Storage area for iron in macrophage.

alpha-methene bridge

Protoporphyrin ring is made up of what bridge?

Kidneys; urobilin

Breakdown of Hb:

Hb will return to the circulation through what organ and as what pigment

urobilin and stercobilin

Breakdown of Hb:

Hb will be excreted as feces and as what pigment

EMBRYONIC HEMOGLOBINS

Hb at first 3 months after conception

HbF

Major Hb of the fetus and the newborn infant

After birth, smaller amounts of HbF are produced

6 months = HbF is ? than ?

After age 2 years = HbF ? than ?

Adults = ? than ?

Deoxyhemoglobin (HbCO2)

Dark red

Reduced form of Hb

The CO2 binds to the free amino group of the Hb to form carbaminohemoglobin

Color?

NaOH test

Composition: 40% NaOH + EDTA-blood

Positive reaction: Red: (+) НьСO

Negative reaction: Black-Brown: (+) HbO2

Rapid test for HbCO

Requires warming gently (incubation or hand)

Composition:

Positive reaction:

Negative reaction:

Sulfhemoglobin

pyrrole ring

0.5 g/100 ml

Mauve-lavender and Heinz bodies

600-620 nm

Hb with sulfur attachment

Occurs to drugs with sulfur compounds like in laxative drugs

Occurs with chronic constipation

MOST DANGEROUS

The pathway sulfur of hemoglobin is via ___

Critical Value: ___

Indicated by: ___ and ___

Absorption: ?

TRUE

(CN) + NO2 → Hi + CN (they have affinity w each other) → HiCN poisoning (cannot carry oxygen)

TRUE OR FALSE

Methemoglobin has strong affinity with cyanide

Methemoglobin, Carboxyhemoglobin (irreversible if reached the critical values)

These are your reversible to oxyhemoglobin type of Hb:

Ferrous

Most Iron in the body must be in ___ state

Fe2+

iron that allow binding of O2 to Hb for transport to lungs and body tissues

Ferric iron (Fe3+)

iron that is not able to bind hemoglobin but binds to transferrin

TRUE

TRUE OR FALSE

If exposed to oxidants: Fe2+ oxidized into Fe3+

FALSE

It will affect Hb synthesis, no one will transport Fe2+

TRUE/FALSE

Fe3+ will not affect the Hb synthesis because if it binds to transferrin, it will transport Fe2+

Serum Iron

measures the amount of Fe bound to transferrin

Measures how much iron attach to transferrin

Total Iron binding Capacity (TIBC)

total amount of iron that transferrin can bind when fully saturated

Measures how much of iron can saturate 1 TIBC

Serum ferritin

indirect measurement of storage iron in tissues and BM

reduced Diphosphopyridine dinucleotide (DPNH)

methemoglobin reductase

maintains iron in a ferrous state; can only produce if there is _____

Methemoglobin reductase or diaphorase

responsible for the production of DPNH

Methemoglobin reductase deficiency

cannot produce DPNH = Fe3+ produced because no one will maintain iron in ferrous state

reduced Diphosphopyridine dinucleotide, reduced Triphosphopyridine nucleotide, · Ascorbic acid

MAINTENANCE OF HEMOGLOBIN IN THE NORMAL REDUCED STATE is seen with these proteins:

reduced Triphosphopyridine nucleotide (TPNH)

Glucose-6-PO4 dehydrogenase

Production of____ in the presence of ____ → Reduced Glutathione

Reduced glutathione

supply the body or source with TPNH

Ascorbic acid

Aside from DPNH and TPNH, what else can reduce Fe3+ to Fe2+

INHERITED ENZYME DEFICIENCY, INHERITED M, ACQUIRED (TOXIC METHEMOGLOBINEMIA)

3 Conditions associated with Methomoglobinemia