finals - proteins Flashcards

1
Q

protein came from a greek word __

A

proteis

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2
Q

Protein comes from the greek word proteis, meaning___

A

“first rank of importance.”

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3
Q

proteisn are synthesized in the __and secreted by the hepatocyte into the circulation except immunoglobulins (plasma cells).

A

liver

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4
Q

amino acids are protein’s building block, how do amino acids are linked together

A

covalently

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5
Q

Proteins can bear positive and negative charges which means they are __

A

amphoteric

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6
Q

They can be both a weak base or weak acid, hence,
proteins are effective ___.

A

blood buffers

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7
Q

longer chain but lower than 1 k chains

A

oligopeptide

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8
Q

1k chain

A

polypeptide

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9
Q

protein’s solubility is due to ___

A

high dielectric property

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10
Q

They are very effective antigens due to their
___.

A

molecular mass, tyrosine content and their specificity

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11
Q

They provide __of the total daily body energy
requirement.

A

12 to 20%

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12
Q

Proteins are ____% of the cell’s dry weight

A

50% to 70

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13
Q

elements of protein

A

CHO - N

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14
Q

additional elements of protein aside from CHON

A

sulfur, iron, phosphorous, and other metals

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15
Q

It is the fact that proteins contain __ that sets
them apart from pure carbohydrates and lipids, which
do not contain nitrogen atoms

A

nitrogen

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16
Q

The nitrogen content of serum protein is, on average,approximately __

A

16%.

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17
Q

This measurement of ___ is used in one
method for total protein

A

nitrogen content

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18
Q

a type of technique that measures Nitrogen that is directly proportional to the concentration of the total protein in the body

A

kendal daw

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19
Q

Most versatile molecules in our bodies

A

proteins

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20
Q

how many different proteins exist in our bodies

A

10,000-50,000

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21
Q

Amino Acids are large molecules that is why they are termed as

A

macromolecules

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22
Q

Fundamental building blocks of all proteins

A

Amino Ac

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23
Q

Electric charge depends on __

A

pH of the solution and type of R group

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24
Q

amine group elements

A

NH2

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25
Q

carboxyl group elements

A

COOH

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26
Q

amine group and carboxyl group is held together by

A

chiral carbon

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27
Q

the group which is responsible for the specificity of amino acid

A

r group

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28
Q

electric charge of basic or carboxylic group

A

negative

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29
Q

electric charge of acidic or amine group

A

positive

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30
Q

Basic solution – (-) charge, proton ___ from the
carboxyl group present forming COO

A

dissociate

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31
Q

Acid solution excess of protons (H+) which can attach to NH2 group to form ___

A

NH3+

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32
Q

These charges affect how each protein moves in an ___ -

A

electric field

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33
Q

the movement of proteins are based on

A

electric charges

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34
Q

it allow us to separate proteins based on the electric charges

A

SPE - serum protein electrophoresis

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35
Q

Both (+) and (-) charges may exist on the same
molecule

A

Zwitterion

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36
Q

netcharge of Zwitterion

A

neutral or 0

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37
Q

sum of molecules
charges equals zero.

A

isoelectric point

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38
Q

normal pH of protein is

A

5.5 - 8

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39
Q

once the protein is subjected to SPE the solution’s pH must be

A

8.6

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40
Q

Functions of proteins

A
  1. Repair body tissues
  2. Important in blood coagulation and immunologic function
  3. For transport of metabolic substances
  4. Maintenance of osmotic pressure
  5. Maintenance of blood pH (buffers)
  6. Biocatalysts
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41
Q

in coagulation process, proteins are made up of

A

serine proteases

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42
Q

term referred to space inside the vessel

A

intravascular space

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43
Q

term referred to space outside the vessel

A

extravascular

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44
Q

extravasation of blood fluid

A

edema

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45
Q

Four Structures of Proteins

A

Primary Structure
Secondary Structure
Tertiary Structure
Quaternary Structure

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46
Q

It is the linear sequence of the amino acid.

A

. Primary Structure

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47
Q

It determines the Identity of protein, molecular
structure, function binding capacity and recognition
ability.

A

Primary Structure

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48
Q

Any change in the amino acid composition can
significantly alter the protein.

A

Primary Structure

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49
Q

It involves the winding of the polypeptide cha

A

. Secondary Structure

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50
Q

It refers to specific 3-dimensional conformations -
alpha helix, beta pleated and bend form

A

Secondary Structure

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51
Q

How the protein chain twists and bends along its
length

A

alpha helix
beta pleated sheet
random

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52
Q

Secondary Structure

coil, resembling a spring

A

alpha helix

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53
Q

Secondary Structure

flat, corrugated structure

A

beta pleated sheet

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54
Q

Secondary Structure
no apparent pattern

A

random

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55
Q

It is the actual 3-dimensional configuration, the folding
pattern of the protein.

A

tertiary Structure

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56
Q

It is responsible for many of the physical and chemical
properties of the proteins.

A

Tertiary Structure

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57
Q

It is maintained by electrovalent linkages, hydrogen
bonds, disulfide bridges, Van der Waals forces and
hydrophobic interactions.

A

Tertiary Structure

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58
Q

It is the association of 2 or more polypeptide chains to form a functional protein molecule.

A

Quaternary Structure

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59
Q

Example of quaternary structure h

A

hemoglobin, LDH, CPK

lactate dehydrogenase
creatinine phosphokinase

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60
Q

Classes of Proteins according to Functions

A
  1. Enzymes
  2. Structural proteins
  3. Contractile proteins
  4. Antibodies
  5. Transport proteins
  6. Peptide hormones
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61
Q

a transport protein that has no quarternary structure - single polypeptide

A

Albumin

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62
Q

are those that generate
precursors of glucose such as pyruvate or citric acid
cycle intermediates.

A

Glucogenic amino acids

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63
Q

are degraded to acetyl-CoA
such as leucine or lysine.

A

Ketogenic amino acids

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64
Q

how do we able to convert amino acids to glucose

A

gluconeogenesis

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65
Q

Example of glycogenic amino acid:

A

alanine (pyruvate),
arginine (a- ketoglutarate),
aspartate

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66
Q

Classification of Proteins according to Fu

A

Simple Protein
Conjugated Proteins

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67
Q

2 types of simple proteins

A

fibrous or globular

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68
Q

They contain peptide chains which on hydrolysis yield
only amino acids.

A

Simple Proteins

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69
Q

example of fibrous simple protein

A

fibrinogen, collagen

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70
Q

example of globular simple protein

A

hemoglobin, plasma proteins, peptide
hormones

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71
Q

are compact and have
little or no space for water in the interior of the molecule; they retain their biological activities within
narrow ranges of temperature and pH.

A

globular proteins

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72
Q

These are composed of a protein (apoprotein) and a
non-protein moiety (prostheticgroup).

A

Conjugated Proteins

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73
Q

the protein part of conjugated protein is calld as

A

apoprotein

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74
Q

the nonprotein part of conjugated protein is calld as

A

prosthetic group

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75
Q

a conjugated proteins

example of Metalloproteins

A

ferritin,
hemoglobin and flavoproteins

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76
Q

a conjugated proteins

example of Lipoproteins

A

VLDL, HDL, LDL, chylomicrons

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77
Q

a conjugated proteins

example Glycoproteins

A

haptoglobin, ar-antitrypsin (with
10%-40% CHO)

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78
Q

a conjugated proteins

example Mucoproteins or proteoglycan

A

mucin (higher
CHO content than CHON)

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79
Q

a conjugated proteins

example Nucleoproteins

A

chromatin

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80
Q

is a balance between anabolism
(synthesis) and catabolism

A

Nitrogen balance

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81
Q

It is when a protein catabolism
exceeds anabolism

A

Negative nitrogen balance

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82
Q

It is characterized by excessive
tissue destruction such as burns,
wasting disease, high fever and
starvation

A

Negative nitrogen balance

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83
Q

It is when anabolism is greater than
catabolism

A

Positive nitrogen balance

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84
Q

Positive nitrogen balance example are

A

growth, pregnancy and
repair processes

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85
Q

It migrates ahead of albumin

A

Prealbumin

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86
Q

Prealbumin alias

A

Transthyretin

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87
Q

It is rich in tryptophan and contains 0.5%
carbohydrate.

A

Prealbumin (Transthyretin

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88
Q

t4 alias

A

Thyroxine

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89
Q

half life of pre albumin

A

2 days

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90
Q

secondary structure of pre albumin

A

B-pleated sheet conformation

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91
Q

Prealbumin (Transthyretin) aliases

A

retinol-binding protein.
thyroxine binding globulin

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92
Q

It is used to detect malnutrition and individual’s
response to dietary supplementation

A

Prealbumin (Transthyretin

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93
Q

It is used as landmark to confirm that the specimen is
really CSF it crosses more easily into the CSF than
other proteins

A

Prealbumin (Transthyretin)

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94
Q

Prealbumin (Transthyretin) increased in

A

alcoholism, chronic renal failure, steroid
treatment

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95
Q

Prealbumin (Transthyretin in Decreased

A

poor nutrition

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96
Q

ref value of pre albumin

A

18-45 mg/dl :

Conversion factor: 10-
mg/L

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97
Q

retinol is also known as Vit ___

A

A – VITAMIN A

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98
Q

It is the most abundant protein in the plasma.

A

Albumin

99
Q

It serves as a mobile repository of amino acids for
incorporation into other proteins.

A

Albumin

100
Q

It is the general transport protein or carrier.

A

Albumin

101
Q

Albumin half life

A

17 days

102
Q

Elevations of serum albumin concentration occur in

A

✓ Dehydration
✓ Prolonged application of tourniquet for
venipuncture (artifactual hyperalbuminemia)

103
Q

Measurements of albumin concentrations are
important in interpreting __ and___ and magnesium
levels because these ions are bound to albumin.

A

calcium and magnesium

104
Q

Dye Binding methods for albumin measurements employ ___-

A

✓ Bromocresol Green (BCG)
✓ Hydroxyozobenzene Benzoic Acid (HABA)

105
Q

The presence of albumin in the urine is considered

A

abnormal even in small amounts.

106
Q

It is the protein present in highest concentration in plasma

A

albumin

107
Q

A general transport protein (binds various substances in
the blood).

A

albumin

108
Q

It Is a sensitive and highly prognostic marker in cases of
cystic fibrosis

A

albumin

109
Q

It is a “negative acute phase reactant”

A

albumin

110
Q

a process wherein there’s a decrease in
acute inflammatory processes.

A

negative acute phase reactant

111
Q

Lowest plasma albumin levels are seen in active ___

A

nephrotic syndrome

112
Q

nephrotic
syndrome is a diarrhea of

A

albumin and fats

113
Q

ref of albumin

A

3.5-5.0 g/dl

(CF: 10-g/L)

114
Q

it’s a tight fitting cells that filters protein

A

podocytes

115
Q

It serves as circulating reservoir of amino acids.

A

albumin

116
Q

It is a group of proteins consists of a1, a2, B, and y fractions.

A

Globulin

117
Q

It is usually measured by subtracting the value of serum
albumin from the total protein concentration.

A

Globulin

118
Q

Globulin

Elevated concentration in early ___ will balance
loss of albumin resulting to normal levels of total protein.

A

cirrhosis

119
Q

Measurement of globulin

A

Total Protein - Albumin = Globuli

120
Q

Globulin ref range

A

2.3-3.5 g/dl

CF: x10 g/L
23-35 g/L)

121
Q

It is an acute-phase reactant, a glycoprotein.

A

Antitrypsin (AAT)

122
Q

It neutralizes trypsin-like enzymes (like neutrophil elastase) - this enzyme is released from WBCs to combat infection but it can also destroy alveoli which can lead to emphysema.

A

Antitrypsin (AAT)

123
Q

ASSOCIATED TO EMPHYSEMA

A

al-Antitrypsin (AAT)

124
Q

It is a major inhibitor of protease activity - prevents
self-destruction of tissues.

A

al-Antitrypsin (AAT)

125
Q

It comprises 90% of the al-globulin band.

A

al-Antitrypsin (AAT)

126
Q
A
127
Q

al-Antitrypsin (AAT) Increased:

A

inflammation, pregnancy and
contraceptive use

128
Q

DEFICIENCY OF al-Antitrypsin (AAT) WILL LEAD TO

A

emphysematous pulmonary disease and
juvenile hepatic cirrhosis

129
Q

ref range of AAT - al-Antitrypsin (AAT)

A

145-270 mg/dL (CF: 0.01-g/L)

130
Q

what is the movement of alpha feto-protein in electrophoresis

A

migrates between albumin and a
1 globulin ba

131
Q

is afp a glycoprotein?

A

yes

132
Q

It is synthesized initially by the fetal yolk sac and then
by the fetal parenchymal cells of the liver.

A

AFP

133
Q

It is the most abundant protein in fetal serum

A

afp

134
Q

afp

It peaks in the fetus at ___ weeks of gestation.

A

13

135
Q

afp

It is detectable in the maternal blood up to the ___ month of pregnancy - maternal serum

A

7th or 8th

136
Q

AFP is ___ in the presence of twins (transmitted across the placenta).

A

increased

137
Q

do afp has known function in adults?

A

it has no known function in adults

138
Q

Specimen for AFP testing

A

maternal serum; amniotic fluid; serum (for
cancer screening)

139
Q

Method for testing afp

A

immunochemical test (using monoclonal
antibodies against AFP), RIA and EIA

140
Q

afp is a marker of __ in adult patient

A

cancer

141
Q

ref range of afp

A

5 ng/ml (adult and children sera)

142
Q

Maternal serum AFP is used to detect __ in a fetus or child

A

neural tube defect or down syndrome

143
Q

Maternal AFP screening for NTD and DS is done between ___ weeks’ gestational age when the maternal serum increases gradually.

A

15 and 20

144
Q

AFP is also used as a tumor marker for ____.

A

hepatic and gonodal cancer

145
Q

what are the example of NTD

A

anencephaly, spina bifida,

146
Q

afp is increased in

A

hepatoma (> 1000 ng/ml), NTDs,
anencephaly, spina bifida, atresia of the GIT. fetal distress, ataxia telangiectasia, tyrosinosis, and hemolytic disease of the newborn (HDN)

147
Q

afp is decreased in

A

Down syndrome and trisomy 18

148
Q

al-Acid Glycoprotein is also known as

A

orosomucoid

149
Q

al-Acid Glycoprotein /orosomucoid

It contains high percentage of ___ and ____ (45% ___ + 11-12% _____).

A

CHO; sialic acid

150
Q

al-Acid Glycoprotein /orosomucoid

it is ___ charged even in acid
solution.

A

negatively

151
Q

alpha - acid glycoproitein/orosomucoid

It has greatest affinity for ___; binds
quinidine (cardioactive drug)

A

progesterone

152
Q

It is a useful diagnostic tool in neonates with bacterial infections

A

al-Acid Glycoprotein /orosomucoid

153
Q

al-Acid Glycoprotein /orosomucoid

its amino acid sequence is similar with
__

A

immunoglobulin

154
Q

al-Acid Glycoprotein /orosomucoid

Increased in ___

A

pregnancy, cancer, pneumonia,
rheumatoid arthritis (RA) and cell proliferation

155
Q

al-Acid Glycoprotein /orosomucoid (AAG)

ref range

A

55-140 mg/dL (CF: 0.01-g/L)

156
Q

It is a serine proteinase with cathepsin G; acute phase reactant.

A

al-Antichymotrypsin (al-x)

157
Q

al-Antichymotrypsin (al-x

It migrates between the ___ zones;
synthesized in the liver

A

a1 and a2

158
Q

It binds and inactivates prostate-specific antigen (PSA) - PSA complexed with al-x is

A

. al-Antichymotrypsin (al-x)

159
Q

It is the major form of PSA found in human sera.

A

al-Antichymotrypsin (al-x)

160
Q

It is associated with the pathogenesis of Alzheimer’s disease - al-xis a vital component of the amyloid deposits found in persons with such disorder.

A

al-Antichymotrypsin (al-x)

161
Q

al-Antichymotrypsin (al-x) increases in what conditions

A

infection, malignancy, burn, AMI and
Alzheimer’s disease

162
Q

al-Antichymotrypsin (al-x) deficiency will result in

A

liver disease

163
Q

al-Antichymotrypsin (al-x) reference valu

A

30-60 mg/dL (CF: 0.01-g/L)

164
Q

It binds heme released by degradation of hemoglobin - has the strongest affinity for heme

A

Hemopexin

165
Q

It helps in the diagnosis of early hemolysi

A

Hemopexin

166
Q

Hemopexin

It migrates in the ___ region during electrophoresis.

A

beta

167
Q

Hemopexin ref range

A

50-115 mg/dL (CF: 0.01-g/L

168
Q

it exhibits affinity with vitamin D and actin (vitamin D binding protein)

A

Group-specific component

169
Q

Group-specific component (Gc)-Globulin

It migrates in the___ interzone during
electrophoresis

A

a-1 and a-2

170
Q

Group-specific component (Gc)-Globulinis also known as

A

vitamin D
binding protein

171
Q

manner of testing for Group-specific component (Gc)-Globulin is

A

Radial immunodiffusion

172
Q

ref range of . Group-specific component (Gc)-Globulin

A

20-55 mg/dL (CF: 0.01-g/L)

173
Q

is Haptoglobin ssynthesized in the hepatocytes?

A

yes

174
Q

is Haptoglobin an apr?

A

yes

175
Q

It binds free hemoglobin by its a chain

A

Haptoglobin

176
Q

It prevents the loss of hemoglobin and its constituent
iron into the urine

A

Haptoglobin

177
Q

It is a useful measurement for serially monitoring
patients who have a slow but steady rate of red cell
breakdown such as by mechanical heart valves,
hemoglobinopathies, or exercise- associated trauma

A

Haptoglobin

178
Q

It evaluates degree of intravascular hemolysis (HTR
& HDN).

A

Haptoglobin

179
Q

Haptoglobin

Its plasma level is slightly ___ after blood transfusion.

A

decreased

180
Q

haptoglobin

It is also one of the proteins used to evaluate
__ diseases.

A

rheumatic

181
Q

haptoglobin increases in what conditions

A

stressful conditions, myoglobinuri

182
Q

haptoglobin increases in what conditions

A

intravascular hemolysis and hemoglobinuria

183
Q

method of testing of Haptoglobin

A

radial immunodiffusion and immunonephelometry

184
Q

reference value of haptoglobin

A

26-185 mg/dl (CF: 0.01-g/L)

185
Q

It is a copper-binding glycoprotein that has enzymatic
activities

A

ceruloplasmin

186
Q

ceruloplasmin is synthesized in the liver, where___ atoms of
copper are attached

A

6 to 8

187
Q

It imparts a blue color to protein

A

ceruloplasmin

188
Q

ceruloplasmin

It is a marker for ___disease (0.1g/L of
ceruloplasmin).

A

Wilson’s

189
Q

ceruloplasmin

Clinical features of Wilson’s disease:

A

deposition of copper in skin, liver, brain and cornea (Kayser Fleisher rings)

190
Q

deposition of copper in the cornea is known as

A

(Kayser Fleisher rings)

191
Q

Increased ceruloplasmin are can as well be seen in

A

inflammation, cancer and
pregnancy

192
Q

decrease of ceruloplasmin are seen in what conditions?

A

Wilson’s disease, malnutrition,
malabsorption, nephritic disease and Menkes kinky
hair syndrome

193
Q

method of testing ceruplasmin

A

Copper oxidase activity

194
Q

reference value of ceruloplasmin

A

18-45mg/dL CF: 10mg/L

195
Q

It is the largest major nonimmunoglobulin protein in plasma.

A

a2-Macroglobulin (AMG

196
Q

It is found principally In the intravascular spaces; it does not diffuse from the plasma space; lower
amounts can also be found in CSF

A

a2-Macroglobulin (AMG)

197
Q

It inhibits proteases such as trypsin, pepsin and
plasmin.

A

a2-Macroglobulin (AMG)
* It is the largest m

198
Q

It increases 10x in nephrosis - the loss of AMG into
urine is prevented by its large

A

a2-Macroglobulin (AMG)

199
Q

It forms a complex with prostate-specific antigen
(PSA)

A

a2-Macroglobulin (AMG

200
Q

a2-Macroglobulin (AMG increases in what conditions

A

nephrotic syndrome, diabetes and liver
disease

201
Q

method of testing of a2-Macroglobulin (AMG)

A

radial immunodiffusion,
mmunonephelometry, ELISA and latex agglutination

202
Q

ref range of a2-Macroglobulin (AMG)

A

150-420 mg/dL (CF: 0.01-g/L)

203
Q

It is a light chain component of the major human
leukocyte

A

B2-Microglobulin

204
Q

It is found on the surface of most nucleated cells;
present in high concentration on lymphocytes.

A

B2-Microglobulin

205
Q

It is needed in the production of CD8 cells

A

B2-Microglobulin

206
Q

It is freely filtered at the glomerulus, and then is
reabsorbed and metabolized completely by the
proximal tubule elevated plasma levels are the result
of impaired clearance by the kidneys or over
production of proteins as seen in inflammatory
diseases (RA and SLE).

A

B2-Microglobulin

207
Q

it appears in the urine when reabsorption is
incomplete because of proximal tubular damage, as
in acute kidney injury

A

B2-Microglobulin

208
Q

t has a tendency to fold into a B-sheet configuration,
resulting to amyloid formation - it is a common cause
of dialysis-associated amyloidosis.

A

B2-Microglobulin

209
Q

B2-Microglobulin increases in

A

renal failure, multiple myeloma, rheumatoid arthritis (RA). erythematosus (SLE), and HIV

210
Q

Method of testing of b2 microglobulin

A

immunoassay

211
Q

ref range of b2 microglobulin

A

0.2-2.8 ug/dL

212
Q

It is a major component of the Bz-globulin fraction
(electrophoresis).

A

Transferrin (Siderophilin)

213
Q

transferrin is also known as

A

siderophilin

214
Q

It transports iron to its storage sites; CSF contains
small amount.

A

Transferrin (Siderophilin)

215
Q

It is used to determine the cause of anemia, to
measure iron metabolism and determine the iron
carrying capacity of the blood

A

Transferrin (Siderophilin)

216
Q

It prevents loss of iron through the kidneys

A

Transferrin (Siderophilin)

217
Q

trasnferrin

In ___ anemia, its concentration is normal
or increased.

A

iron deficiency

218
Q

Low plasma transferrin can impair hemoglobin
production and lead to _.

A

anemia

219
Q

Deficiency of transferrin may result in the
accumulation of iron in apoferritin or in histiocytes, or
precipitates in tissues as ___.

A

hemosiderin

220
Q

Increased transferrin will lead to

A

hemochromatosis (bronze-skin), ID

221
Q

decreased transferrin will lead to

A

liver disease, malnutrition, nephrotic
syndrome

222
Q

method of testing for transferrin

A

Immunodiffusion and immunonephelometry

223
Q

ref range for transferrin

A

✓ Male 215-365 mg/dL (CF: 0.01-g/L)
✓ Female = 250-380 mg/dL (CF: 0.01-g/L)

224
Q

“These are synthesized in the plasma

A

Immunoglobulins

225
Q

immunoglobulins are These are glycoproteins composed of

___ proteins, and
__ carbohydrate produced by
white blood cells known as B cells, that confer
humoral immunity

A

82% to 96%;4% to 18%

226
Q

Ig are increased in what conditions

A

hepatic
disease,
infections,
toxoplasmosis, cytomegalovirus infections, rubella
herpes, syphilis, allergic reactions, multiple myeloma

227
Q

method of testing in Ig

A

nephelometry, turbidimetry, radial
immunodiffusion and immunoassay

228
Q

it binds with proteins and lipids forming LDL, HDL,
VLDL and chylomicrons.

A

Lipoprotein

229
Q

it is one of the largest proteins in the blood.

A

Fibrinogen

230
Q

It is the most abundant of the coagulation factor - it
forms a fibrin clot when activated by thrombin

A

fibrinogen

231
Q

It may serve as a marker for long-term prognosis of
cardiovascular disease.

A

fibrinogen

232
Q

High levels in plasma may cause elevated erythrocyte
sedimentation rate (ESR) - by coating the cells
andallowing them to sediment faster in clumps.

A

fibrinogen

233
Q

fibrinogen increased in what conditions

A

inflammatory disorders, pregnancy and
used of birth control pills

234
Q

Decreased fibrinogen are seen in

A

extensive coagulation

235
Q

ref range of fibrnogen

A

Reference value: 200-400mg/dL (2.0-4.0 g/L

236
Q

___(and also C4) concentration is a convenient
marker for assessing disease activity in rheumatic
disorders such as RA and SL

A

C3

237
Q

It is a member of pentraxin protein family

A

C-reactive protein (CRP)

238
Q

CRP was so named because it binds to the C
polysaccharide of the pneumococcus it precipitates with the C substance, a polysaccharide of
pneumococci.

A

c reactive protein

239
Q

It is a general scavenger molecule; gamma-migrating
protein.

A

c reactive protein

240
Q

It is a cardiac marker - used as an early warning test to persons at risk of coronary artery diseas

A

c reactive protein

241
Q

It is an inflammatory marker that appears to reflect the
severity of CHD and may contribute to its
pathogenesis

A

c reactive protein

242
Q

c reatcive protein increases in

A

acute rheumatic fever, myocardial
infarction (MI), RA, gout, bacterial and viral infection

243
Q

Reference value of c reactive protein:__

A

< 1.0 mg/dl

244
Q
A