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ISBB > Fundamentals of Blood Banking > Flashcards

Fundamentals of Blood Banking Flashcards

1
Q

Crucial Areas for Normal RBC Survival and
Function

A
  1. Normal Chemical Composition and Structure
  2. Haemoglobin Structure and Function
  3. Red Cell Metabolism Pathways
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2
Q

Any defects in any or all of the areas necessary for RBC survival and function would result in

A

RBCs surviving less than 120 days.

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3
Q

Components of Red cell membrane

A

52% Protein
40% Lipids
8% Carbohydrates

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4
Q

1.) Main Lipid component of RBC
2.) Main protein responsible for deformability
3.) Evidence for loss of deformability
4.) Calcium Binding protein

A
  • Phospholipids
  • Spectrin
  • Formation of Spherocytes and Bite Cells.
  • Calmodulin
    • spherocyte - Rbc with no central pallor
    • bite cells - bitten apple appearance.
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5
Q

T/F:

I. The lipid component of RBC is semi-permeable
II. It contains hydrophobic heads and hydrophilic tails

A

I is true, II is false

  • hydrophilic heads - hydrophobic tails
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6
Q

T/F:

I. Lipids and proteins are symmetrically distributed in the RBC
II. The hydrophobic heads of the lipids faces the interstitial fluid and cytosol

A

BOTH ARE FALSE

  • asymmetrically distributed
  • hydrophilic heads
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7
Q

Responsible for the cytoskeletal structure of RBC

A

Protein mesh-like cytoskeleton/ RBC membrane protein

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8
Q

Responsible for the cytoskeletal structure of RBC

A

Protein mesh-like cytoskeleton/ RBC membrane proteins

*specifically peripheral proteins

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9
Q

An rbc membrane protein that is FOUND BENEATH THE LIPID LAYER (in the cytoplasmic surface of the membrane) and forms the cytoskeleton.

A

Peripheral Proteins

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10
Q

Two kinds of RBC membrane protein

A

Integral proteins
- span the entire rbc membrane to the cytoplasm

Peripheral proteins
- beneath the lipid bilayer
- forms the cytoskeleton

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11
Q

Are examples of Integral proteins

A

Glycophorin A, B, C and Anion-exchange channel protein

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12
Q

An rbc membrane protein that Extends from outer surface and span the entire RBC membrane to the cytoplasm.

A

Integral proteins

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13
Q

Are examples of Peripheral proteins

A

Band 5 -spectrin, actin
2.1 - Ankyrin
Adducin
Bands 4.1, 4.2 and 6

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14
Q

This refers to the migration patterns of the proteins in Sodium Dodecyl Sulfate (SDS) Polyacrylamide Gel Electrophoresis.

A

Band numbers in rbc membrane proteins

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15
Q

Chemical Composition and Structural Arrangement of RBC Membrane maintain critical roles in 2
important RBC characteristics:

A

Deformability and Permeability.

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16
Q

Refers to the ability of the RBC to be BENT OR STRETCHED out in order to avoid lysis when passing through narrow openings.

A

Deformability

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17
Q

Loss of ATP (energy) and accumulation of membrane calcium results to

A

Loss of deformability/pliability

loss of ATP = decreased phosphorylation of spectrin
↓
accumulation of Ca and Na
↓
dehydrated and rigid cell
↓
sequestration of abnormal rbc in spleen
↓
decreased RBC survival

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18
Q

It poses a marked disadvantage when passing through Small Sinusoidal Orifices (3-5 um in diameter) of the Spleen

A

Loss of Deformability/Pliability

  • kay ma abnormal rbc naman siya (either ma spherocyte or bite cell) then isequester/remove sa spleen mao to mo decrease pud ang rbc survival
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19
Q

Ability of the RBC Membrane to ALLOW SUBSTANCES TO PASS THROUGH in and out of the membrane.

A

Permeability
- prevents colloid hemolysis and controls rbc volume

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20
Q

T/F:

I. Rbc must be FREELY PERMEABLE to Water and Anions (Chloride and Bicarbonate).
II. Relatively impermeable to Cations (Sodium and Potassium).

A

Both are true

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21
Q

Form of hemoglobin that has lesser affinity for oxygen

A

Tense form/ T-form

Hgb w/ O2
↓
unloading of O2 to tissues
↓
Deoxyhemoglobin (hgb w/out O2)
↓
2-3 DPG binds to hgb
↓
Formation of Anionic salt bridges
↓
Tense form conformation
↓
Lower affinity to oxygen

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22
Q

Main function of hemoglobin

A

Gas transport
- O2 transport to tissues
- CO2 excretion

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23
Q

refer to Allosteric Changes (T and R forms) that occurs as hemoglobin loads and unloads oxygen.

A

Respiratory movement

24
Q

Form of hgb that has higher affinity for Oxygen

A

Relaxed form

Deoxyhgb w/ salt bridges (tense hgb)
↓
hgb takes up O2
↓
salt bridges are broken
↓
2-3 DPG are expelled
↓
relaxed conformation
↓
higher affinity of hgb to O2

25
Q

T/F:

I. An increase in 2-3 DPG results to lesser affinity of hgb to O2 thus increasing the delivery of oxygen to tissues
II. This phenomenon causes a shift to the left in the hemoglobin dissociation curve

A

I is true, II is false

*increase 2-3 DPG
↓
lesser affinity of hgb to O2
↓
meaning: increase delivery of O2 to tissues
↓
Shift to the right

Note:
Shift to the left if
↓
high affinity og hgb to O2
↓
thus decreasing delivery of O2 to tissues.

26
Q

Factors affecting increase delivery of oxygen to tissues (shift to the right)

A

Hypoxia and anemia as well as:
↑
- 2-3 DPG
- temperature
- CO2 (haldane effect)

↓
- pH (acidic/ bohr effect)

Bali ra sa shift to the left pero wla si hypoxia and anemia then presence of ABNORMAL hgb

27
Q

Main metabolic pathway of RBC responsible for ATP production

A

Embden-Meyerhof Pathway (Anaerobic Glycolytic Pathway)
- 90% ATP
- start: glucose
- end product: lactate/ lactic acid

28
Q

Metabolic pathway responsible for the formation of Reduced Glutathione (GSH) that protects RBCs from hemolysis by oxidative free radicals and
reduces oxidized sulfhydryl groups in haemoglobin.

A

Pentose Phosphate Pathway
-Hexose Monophosphate Shunt
- 10% ATP
- uses enzyme: G6PD

29
Q

Metabolic pathway responsible for the conversion of ferric ions of Methemoglobin to ferrous ions to form
Functional Hemoglobin.

A

Methemoglobin Reductase Pathway

30
Q

Enzyme used in Methemoglobin Reductase Pathway

A

Methemoglobin Reductase - aka Diaphorase.

31
Q

Metabolic pathway responsible primarily for the production and accumulation of 2,3-DPG.

A

Rapoport-Luebering Shunt

32
Q

Volume of Whole blood usually used for transfusions.

A

450 ml

33
Q

It is a measure of in vivo RBC survival following transfusion.

A

RBC viability

34
Q

Shift of the right in Hgb dissociation curve

A

Increase delivery
decrease affinity

35
Q

Shift of the left in Hgb dissociation curve

A

Decrease delivery
Increase affinity

36
Q

All of the causes a shift to the right in HGB dissociation curve except;

a.) High temperature
b.) Anemia and hypoxia
c.) Abnormal hgb
d.) Decrease pH

A

C. abnormal hgb

37
Q

Biochemical changes of stored blood (RBC storage lesions)

A

↓
- % of viable cells
- pH (Acidic)
- glucose and ATP
- 2-3 DPG

↑
- lactic acid
- plasma K
- plasma HGB

Shift to the left due to ↓ 2-3 DPG

38
Q

these are preserving solutions added to RBC’s after removal of the plasma with or without platelets.

A

Additive Solutions (AS)

39
Q

T/F:

I. One advantage of using PVC bags is its component called “di(ethylhexyl)-phthalate” (DEHP) which causes
leeching of plastic lipids to lipids of RBC Membrane;
II. It helps Stabilize RBC Membrane and Reduces Hemolysis Extent during storage.
III. PVC bags easily breaks down at HIGH temperature

A

I and II is true, III is false

  • PVC bags easily breaks down at LOW temperature
40
Q

A type of solution preferred when high-hematocrit RBC’s are transfused

A

Additive Solutions

  • lowers hct from 70-85% to 50-60%
41
Q

A bag that contains additive colutions

A

Satellite bag

42
Q

Additive solution that utilizes SAG (Saline, Adenine, and Glucose) or SAG-M (Saline, Adenine,
Glucose and Mannitol)

A

Hodma-Sweden

43
Q

A type of solution in which ATP and 2,3-DPG levels are restored/enhanced by metabolic alterations.

A

Rejuvination solutions/ Rejuvesol

  • isalvage tong mga nadaot na components
44
Q

T/F:

I. RBCs outdated for up to 3 days can be rejuvenated/salvaged depending on what preservative
solution was used.
II. Only RBCs from a 450mL blood collection can be rejuvenated.

A

BOTH are true

45
Q

How to prepare an additive solution

A

100mL of Additive Sol’n / RBC Concentrate prepared from 450mL Blood Collection

46
Q

These are primarily used for autologous units and storage of rare blood types.

A

Red cell freezing/ Frozen RBC’s

47
Q

Most commonly and is a penetrating cryoprotective agent

A

Glycerol

48
Q

Non-penetrating cryoprotective agent

A

Hydroxy-ethyl starch (HES)
- coats the cell only

49
Q

T/F:

I. Glycerol must be added to RBCs rapidly and with vigorous shaking to allow complete permeation to
RBCs.
II. Once thawed, frozen RBCs demonstrate function and viability close to that of fresh blood.
III. Most bloodbanks utilize the LOW-Concentration Glycerol technique.

A

II is true, I and III is false

  • added slowly w/ vigorous shaking
  • High conc. glycerol technique is commonly used
50
Q

This must be performed before transfusion of frozen RBCs to remove glycerol otherwise hemolysis would result.

A

Deglycerolization

51
Q

How is Deglycerolization performed

A

by using Decreasing Concentrations of Saline (12% Saline then 1.6% Saline then 0.2% Dextrose in Saline).

52
Q

Most Common Isolates found in RBC Units which causes greenish coloration in the blood bag

A

Yersinia enterocolitica

53
Q

These results to loss of RBC viability during storage

A

RBC storage lesions
- biochemical changes in stored blood

54
Q

RBC size
Platelet size

A

RBC: 7.5 um (top view); 2.0 um (diameter)
platelet: 2-4 um in diameter

55
Q

Most common isolates found in platelets

A

S.epidermidis and S. aureus

56
Q

Current storage time and storage temperature for plt concentrates and apheresis platelet components

A

5 days at 20-24 (specifically midnight of day 5)

57
Q

What is the lowest allowable pH for platelet component at outdate

A

6.2

ISBB (3 decks)

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