HEMA Hgb Flashcards

1
Q

HEMOGLOBIN

A

Structure
B. Biosynthesis
C. Regulation
D. Functions
E. Derivatives

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

iron bearing protein contained
within the ___ .
it is synthesized by young
___ from the ____ up to _____.
____ can carry ___

A

Hemoglobin
-erythrocytes
-erythroblast
- polychromatophilic normoblast
stage
- reticulocytes stage
- one gram of hemoglobin
- 1.34 ml of oxygen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

1 heme= ___
1 hgb= ____

A

1mole of O
4 moles of 0

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

FUNCTIONS OF
HEMOGLOBIN

A

Transport oxygen from the lungs
to the tissue and carbon dioxide
from the tissue.

Acid – base balance regulation
ph7.35-7.45

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Hemoglobin assist in maintaining the pH of blood by _____, ___ and ___ of ___ ( a regular vascular tone that refers to degree of constriction which blood vessel experience)

A

binding, releasing and transport of nitric oxide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Structure of Heme
Composition of Heme

A
  1. Protophorphyrin IX
    Consists of a ring of :
    Carbon ( C)
    Hydrogen ( H)
    Nitrogen
    2.Ferrous iron (Fe2+)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

The______ comprising each hemoglobin molecule
consist of _____ , 141 to
146 amino acids each.
Each globin ___ separated by ___

A

Globin Structure
- four globin chains
-two identical pairs of unlike polypeptide chains
- 8 helices
-7 non helices segment

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Alpha
Beta
Gamma A
Gamma G
Delta
Epsilon
Zelta
Theta

A

Number of amino acids (important in each globin chain- * if not = problem esp. he,oglobinopathies)
141 (if Adult Hgb 141+ 141 alpha= 282 no more/less)
146
146 (position 136: alanine)
146 (position 136:glycine)
146
146
141
Unknown

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

COMPLETE HEMOGLOBIN
MOLECULE
* The hemoglobin molecule can be described by its
1.
2.
3.
4.

A

COMPLETE HEMOGLOBIN
MOLECULE
1.primary, ——– amino acid sequence
2 Secondary —— helices and non
helices (pleated sheet)
3. Tertiary ——- pretzel like
configuration
4. quaternary ——- complete molecule

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Enzyme involved in Heme synthesis

A

ALA synthase (Aminolevulinic synthase)
ALA dehydralase
Hydroxymethylbilane synthase (PBG deaminase)
Uroporphyrinogen III synthase
Uroporphyrinogen III decarboxylase
Coproporphyrinogen-III oxidase
Protoporphyrinogen III oxidase
Ferrochelatase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Flow of Heme synthesis

A

First step: Condensation- It takes place in mitochondria of Succinyl coA with Glycine w/c catalyzes by ALA synthase to form Amino levulinic acid. This ALA will go out from mitochondria which will go into cytoplasm, by the help of ALA dehydralase which will have multiple transformation/ reaction starting from Porphobilinogen-> hydroxymethylbilane which is catalyzed by Hydroxymethylbilane synthase (PBG deaminase). Then forming uroporphyrinogen III by the help of Uroporphyrinogen III synthase. Then will form COP3 (Coproporphyrinogen III) which will catalyzes by Uroporphyrinogen III decarboxylase, then it will go back to mitochondria to form Protoporphyrinogen III by the COP3 oxidase and eventually form Protoporphyrin IX by Protoporphyrinogen III oxidase.

Last step: In mitochondria, Insertion of Iron w/c will catalyzes by Ferrochelataseto form Heme.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Always be ____ because if oxidize to ___ they can no longer bind to ___
- the oxidize hgb called ___ which can’t carry oxygen

A

Ferrous Iron (Fe2+)
Ferric
Oxygen
Methemoglobin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Occurs in the cytoplasm of __ and
____.
* Polypepdtide chains are manufactured in the ___.
* ____ are made via transcription
of genetic code to mRNA and
translation of mRNA

A

SYNTHESIS OF GLOBIN
normoblast
reticulocytes
ribosomes
Globin protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

ONTOGENY OF GLOBIN SYNTHESIS
Time Region
Type of Globin Gene
Type of Hb
1. 3 weeks of Gestation
2. 5 weeks of Gestation
3. 6-30 weeks of Gestation
4. 30 weeks of Gestation
5. At Birth

A

Yolk Sac
zeta and epsilon
Hb Gower1

Yolk Sac
γ&α
Hb Portland
Hb Gower II

Liver & spleen
α & γ & β
Hb F

Liver
delta
Hb A2

Bone marrow
___
HbA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Hemoglobin Function

A

Oxygen Transport
Carbon dioxide transport
Nitric Oxide transport

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

The function of hemoglobin is to readily bind oxygen molecules in the ___, which requires ____; ____; and_____, which requires low
oxygen affinity.

A

Oxygen Transport
lung
high oxygen affinity
to transport oxygen
to efficiently unload oxygen to the
tissues

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

A second crucial function of
hemoglobin

A

Carbon dioxide transport

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

third function of
hemoglobin involves the
___, ___ and ____. It is secreted by
vascular endothelial cells and causes relaxation of vascular wall smooth muscle and vasodilation .

A

Nitric Oxide transport
- binding, inactivation, and
transport of nitric oxide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

is the ability of hemoglobin to bind or release oxygen . Expressed in terms of the ___ at which hgb is 50% saturated

  1. The relationship between ____ and ____ is described as ODC
  2. _____ relationship of O2 affinity with Hb to pH which states that :
    Inc pH ( alkalosis) = ______
    Dec pH ( acidosis )= _____
A

OXYGEN DISSOCIATION CURVE
- Oxygen Affinity
- oxygen tension
- O2 tension(partial tension) and hemoglobin saturation with oxygen
-Bohr Effect
- Inc Hb affinity for O2
- dec hb affinity for O2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

FACTORS THAT INFLUENCE OXYGEN BINDING
Shift to the left Shift to the right
Temperature
Organic phosphates (2,3 DPG) 2,3-diphosphoglyceric acid
p(CO₂) partial pressure of carbon dioxide
p(CO)
pH

A

Decrease
Increase

Decrease
Increase

Decrease
Increase

Increase
Decrease

Increase
Decrease

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

HB-OXYGEN DISSOCIATION CURVE (Sigmoid curve)

the normal position of curve depends on __, ___, ____, ____

A

Concentration of 2,3-DPG
H+ ion concentration (pH)
CO2 in red blood cells
Structure of Hb

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Right shift (decreases oxygen affinity , more 02 release to the
tissues

A

High 2,3-DPG
Dec body pH
High CO2
HbS

23
Q

Left shift (increases oxygen affinity less 02 release to the
tissues

A

Low 2,3-DPG
HbF
Dec body temperature

24
Q

PHYSIOLOGIC FORMS OF
HEMOGLOBIN

A

Oxyhemoglobin
Deoxyhemoglobin

25
Q

hemoglobin in combination with
oxygen.
gives pinkness to the skin and mucous membrane.
seen in ___

A

Oxyhemoglobin
arterial circulation

26
Q

hgb with iron but no O2 seen in
____
unassociated with oxygen
__ formation

A

Deoxyhemoglobin
venous circulation
cyanosis (bluish nail)

27
Q

NORMAL HEMOGLOBIN

A
  1. Embryonic Hemoglobin
    a. Hgb Gower 1
    b. Hgb Gower 2
    c. Hgb Portland
  2. Fetal Hemoglobin ( HbF)
  3. Hemoglobin A or A1
  4. Hemoglobin A2
  5. Hemoglobin A3
28
Q

Found in normal human embryos
and fetuses with a gestational age of less than ___
Absent at birth

A

Embryonic Hemoglobin
three months

29
Q

Hgb Gower 1

A

Composed of 2 zeta and 2 epsilon globin chains

30
Q

Hgb Gower 2

A

Composed of 2 alpha and 2 epsilon

31
Q

Hgb Portland

A

composed of 2 zeta and 2 gamma

32
Q

the major hemoglobin of the fetus
and newborns
Composed 0f ___ and ___
Produced ___

A

Fetal Hemoglobin ( HbF)
2 alpha and 2 gamma
four months after
conception

33
Q

normal adult hemoglobin
95-97% of hemoglobin in normal
adults produced after 1 yr
onwards composed of __ and __

A

Hemoglobin A or A1
2 alpha (141 AA) and
2 beta chains(146 AA)

34
Q

Constitutes less than 3% of the total hemoglobin
Composed of ____

A

Hemoglobin A2
2 alpha and 2 delta

35
Q
  • degradation product of HbA2
  • composed of ___ and ___
A

Hemoglobin A3
2 alpha and 2 delta

36
Q

ABNORMAL HEMOGLOBIN

A

Hemoglobin S
Hemoglobin C
Hemoglobin E
Hemoglobin H

37
Q

This is the primary hemoglobin in people with ___
- have ____ and ___
causes the red blood cell to deform and assume a sickle shape when exposed to decreased amounts of oxygen.

____ is replaced by ____ in the
6th position of beta chain

A

Hemoglobin S (Sgaval)
- sickle cell disease
- two abnormal beta (βS) chains
- two normal alpha (α) chains.
Glutamic acid
valine

38
Q

About 2-3% of people of ___
descent are heterozygotes for hemoglobin C (have one copy of βC).
seen in ___ - those with two copies of βC).
instead of _____, ____ is in B6
It usually causes a minor amount of ____ and ____

A

Hemoglobin C (Cgal)
-West African
- homozygotes
glutamic acid
lysine
hemolytic anemia
mild to moderate enlargement of the spleen

39
Q

is one of the most common beta
chain hemoglobin variants in the world.
* People who are homozygous of it (have two copies of βE) generally have a___, ____ and ____
* A single copy of it does not
cause symptoms unless it is combined with another mutation, such as the one for ___

A

Hemoglobin E
mild hemolytic anemia
microcytic red blood cells
mild enlargement of the spleen.
beta thalassemia trait

40
Q

an abnormal hemoglobin that occurs in some cases of ____
It is composed of ____ and is
produced in response to a severe shortage of ___

A

Hemoglobin H
- alpha thalassemia
- four beta (β) globin chains
- alpha (α) chains

41
Q

Are acquired hemoglobin variants whose structure has been modified by drugs or environmental chemicals.
do not transport oxygen to the tissue well resulting in __ and ___ .
___, __, and ___

A

CHEMICALLY MODIFIED
HEMOGLOBINS
- cyanosis (30%) and Coma and death (50%)
a. methemoglobin
b. sulfhemoglobin
c. Carboxyhemoglobin

42
Q

Is a form hgb in its ferric state
* Has a ___ color and does not revert to red on exposure to oxygen.
* Peak in the range of ___ at pH __under spectral absorption test.
Causes :
- ____
- ____

A

METHEMOGLOBIN ( HI)
- brownish to bluish
- 620 – 640 nm
- 7.1
- Presence of oxidants
- Genetic deficiency – decrease activity of MethHB

43
Q

Formed by the irreversible oxidation of Hb of certain drugs and chemicals.
examples :
___, ___ and ____
Formed by the addition of hydrogen sulfide to hgb has a
_____.
If it reaches the critical level in the blood it imparts ____-

A

SULFHEMOGLOBIN
a. sulfonomides
b. phenacetin
c. acetanilide
- greenish pigment
- MAUVE LAVENDER

44
Q

SULFHEMOGLOBIN
Usually reported in the following situation
1.
2.
3.
4.

A

Usually reported in the following situation
* 1. Px under prolonged treatment with sulfonamides or
aromatic compounds ( phenacitin, acetanilide )
* 2. Px with severe constipation
* 3. In cases of bacteremia caused by Clostridium
perfringens
* 4. In condition known as enterogenous cyanosis

45
Q

Results from the binding of carbon monoxide to heme iron.
* Hb can combine with carbon monoxide with affinity___ greater than that of Oxygen.
* _____ is termed as silent killer for its colorless gas , odor and patient becomes easily ___.

A

CARBOXYHEMOGLOBIN
- 200 times
- Carbon monoxide
-hypoxic

46
Q

HEMOGLOBIN DETERMINATION

A
  1. Visual Methods
    A. Sahli Method
    B .Dares Method
    c. Hadens Method
    D. Wintrobe
    E.Haldene
    F. Tallquists.
  2. Gasometric Method
  3. Spectronic Method
    A. oxyhemoglobin
    B. Cyanmethemolobin
  4. Automated
  5. Other Methods
    Alkaline
    Specific Gravity
    Comparato
47
Q

quickest method

A

Tallquists

48
Q

lyse RBC by mixing it with hypotonic sol’n

A

Haldene

49
Q

Qualitative screening test based on specific gravity. The density of the
drop of blood is ____ to the amount of hemoglobin it contains.
The principle of the test is that when the drop of donor’s blood dropped into copper sulfate solution becomes encased in a sac of copper proteinate, which prevents any change in the specific gravity for about ___

A

Copper Sulfate Specific Gravity
- directly proportional
- 15 seconds

50
Q

SG of 1.053= __

A

12.5g of Hgb

51
Q

CuSO4 +Blood
If blood floats = ____
If blood sink = ____

A

Inc Sg of CuSO4 > blood (dec hgb)
Inc SG of Blood> CuSO4 (Inc Hgb= good to donate blood)

52
Q

Principle:
Hb will combine and liberate a fixed quantity of O₂. The blood is hemolyzed with ___ and
the gas is collected and measured in a ___

A

Gasometric Method (Oxygen Capacity Method)
- saponin
- Van Slyke apparatus.

53
Q

Colorimetric Methods
A. Visual
1.
2.
3.

A
  1. Direct Matching
  2. Acid Hematin
  3. Alkaline Hematin
54
Q

Colorimetric Methods
B. Photoelectric
1.
2.

A

Oxyhemoglobin method
Cyanmethemoglobin or HiCN method