Unit 5 - Hemoglobin Diseases

Question 1

Oxyhemoglobin

Answer 1

LOADS oxygen in lungs

Question 2

What is the affinity for oxygen of oxyhemoglobin

Answer 2

High

Question 3

What form is oxyhemoglobin in?

Answer 3

R or Relaxed form

Question 4

Deoxyhemoglobin

Answer 4

UNLOADS oxygen in the tissues

Question 5

Affinity for oxygen of deoxyhemoglobin

Answer 5

Low

Question 6

What form is deoxyhemoglobin in?

Answer 6

T or tense form

Question 7

What does 2,3 DPG do?

Answer 7

Changes oxyhemoglobin into deoxyhemoglobin

Question 8

Where does 2,3DPG insert itself?

Answer 8

Between beta chains of molecule to make deoxyhemoglobin

Question 9

What does 2,3DPG do to return hemoglobin into oxyhemoglobin?

Answer 9

Exits space between beta chains of molecule to make oxyhemoglobin

Question 10

When 2,3DPG moves out of deoxyhemoglobin, what is this called?

Answer 10

Respiratory movement that makes hemoglobin act as diaphragm for oxygen

Question 11

What does a shift to the right mean?

Answer 11

Right = Low Affinity, Release of oxygen

Question 12

2,3DPG levels in a shift to the right

Answer 12

Increased levels

Question 13

When does hemoglobin unload more oxygen to tissues?

Answer 13

In a shift to the right
At same given tissue partial pressure of oxygen

Question 14

Conditions causing a shift to the right

Answer 14

Inc metabolism
Inc temperature
Dec pH
Tissue hypoxia
Inc carbon dioxide

Question 15

What is a shift to the left?

Answer 15

Giving up less oxygen to the tissues
Won’t let go

Question 16

If the body is under more restful conditions, what way will the curve shift?

Answer 16

To the left

Question 17

When does hemoglobin unload LESS oxygen to the tissues?

Answer 17

In a shift to the left
At same given tissue partial pressure of oxygen

Question 18

Conditions causing shift to the left

Answer 18

Dec metabolism
Inc pH
Inc abnormal hgb
Dec carbon dioxide

Question 19

Bohr effect

Answer 19

Effect of pH on hgb-O2 affinity

Question 20

More acidic = x affinity for oxygen

Answer 20

Less

Question 21

More acidic = x shift of oxygen

Answer 21

Right

Question 22

Acidic situations = x CO2

Answer 22

Increased

Question 23

As hemoglobin unloads oxygen, what can it accept as a blood buffer?

Answer 23

Hydrogen ion

Question 24

Chemical variant of hemoglobin definition

Answer 24

Hemoglobins with reduced or absent gaseous exchange capacity

Question 25

Examples of chemical variants of hemoglobin

Answer 25

Carboxyhemoglobin Methemoglobin Sulfhemoglobin

Question 26

Carboxyhemoglobin

Answer 26

Carbon monoxide replaces oxygen Less binding sites for oxygen

Question 27

How does CO bond to hgb compare to O2?

Answer 27

CO has a 200x tighter bond than oxygen

Question 28

What color does carboxyhemoglobin produce to the RBC?

Answer 28

Cherry red color

Question 29

What causes carboxyhemoglobin?

Answer 29

Smoking Exhaust fumes from fuel bunring

Question 30

Treatment for carboxyhemoglobin

Answer 30

Treatment with oxygen

Question 31

What happens if carboxyhemoglobin is not treated?

Answer 31

Prolonged anoxia Can be fatal or cause permanent damage

Question 32

Methemoglobin

Answer 32

Chemically oxidized hgb from ferrous to ferric

Question 33

Normally, what percentage of our hemoglobin is methemoglobin?

Answer 33

1%

Question 34

What keeps our percentage of methemoglobin in check?

Answer 34

Methemoglobin reductase

Question 35

What happens if methemoglobin becomes pathologic?

Answer 35

Cyanosis observed

Question 36

What causes methemoglobin

Answer 36

Inherited enzyme deficiency Hemoglobin M Drugs or dyes

Question 37

What does hemoglobin M do?

Answer 37

Mutation that stabilizes Fe+++ state

Question 38

What drugs or dyes cause methemoglobin

Answer 38

Aniline dyes (ink, crayons) Sulfonamides Nitrates Lidocaine

Question 39

Treatment of methemoglobin

Answer 39

Methylene blue or ascorbic acid

Question 40

Sulfhemoglobin

Answer 40

Permanent replacement of oxygen by sulfur

Question 41

Causes of sulfhemoglobin

Answer 41

Sulfur containing cathartics High levels of sulfonamide antibiotics

Question 42

Can routine hemoglobin analysis measure sulfhemoglobin?

Answer 42

NO

Question 43

What is the routine hemoglobin analysis

Answer 43

Cyanmethemoglobin

Question 44

What can cyanmethemoglobin method not do?

Answer 44

Measure sulfhemoglobin

Question 45

What are genetic varaints of amino acid sequence of globin chains

Answer 45

Hemoglobin S Hemoglobin C

Question 46

What are two ways RBCs are removed from circulation

Answer 46

Extravascular destruction Intravascular destruction

Question 47

Example of extravascular destruction

Answer 47

Macrophage removal in the spleen

Question 48

Intravascular destruction example

Answer 48

Hemolysis

Question 49

Three chemical components of hemoglobin

Answer 49

Heme Iron globin

Question 50

When macrophage process RBCs, what components of hemoglobin are conserved?

Answer 50

Amino acids from globulins and Fe conserved for synthesis of new molecules

Question 51

When RBCs are processed by macrophages, what happens to the heme?

Answer 51

Heme is converted into biliverdin Biliverdin converted to bilirubin Bilirubin released to blood for additional processing Liver excretes bilirubin

Question 52

Macrophage processing is what component of hemolysis?

Answer 52

Extravascular

Question 53

Haptoglobin

Answer 53

CirculatingProtein in circulation that conserves free hemoglobin

Question 54

What happens without haptoglobin?

Answer 54

Hgb can pass through the kidneys into urine

Question 55

What happens to prevent hgb excretion?

Answer 55

Hgb-haptoglobin complex forms Too big to be filtered Liver cells take it up

Question 56

What does the liver cells to to hemoglobin?

Answer 56

Processes hemoglobin similar to macrophages

Question 57

What is a marker for IV hemolysis?

Answer 57

Decreased haptoglobin