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CLIN CHEM LEC > AMINO ACIDS AND PROTEINS > Flashcards

AMINO ACIDS AND PROTEINS Flashcards

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1
Q

Building blocks of more complex compounds

A

Amino acid

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2
Q

Amino acids Have three parts

A

Amino group, Side chain or R group, carboxylic acid group

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3
Q

The carbon at the center

A

Alpha - carbon

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4
Q

Their R groups are mostly hydrogen
and carbon

A

○ Non-polar hydrophobic

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5
Q

Their R groups are alcohol, phenol,
thiol, amide

A

polar and charged

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6
Q

Their R group can’t be seen but
supposedly, the oxygen has a
negative charge

A

polar acidic

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7
Q

The negative charge of the oxygen
are one of the signs that describes
the amino acid as __________

A

polar acidic

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8
Q

Instead of having a negative charge,
a positive charge can be seen its side
chains

A

polar basic

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9
Q

sential Amino Acids
- It is required in the diet but cannot be synthesized in the body

A

essential amino acid

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10
Q

give me the essential amino acid

A

P-phenylalanine
V - valine
T - Threonine

T-Trytophan
I - Isoleucine
M - methionine

H - histidine
A - arginine
L - leucine
L - lysine

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11
Q
  • Not required in the diet but can be synthesized by the body
A

Non-essential amino acid

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12
Q

Give me the 12 non-essential amino acid

A

Alanine
● Asparagine
● Aspartic Acid
● Cysteine
● Glutamic Acid
● Cysteine
● Glutamic Acid
● Glutamine
● Glycine
● Proline
● Serine
● Tyrosine

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13
Q

Ala

A

Alanine

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14
Q

Arg

A

Arginine

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15
Q

Asp

A

Aspartic acid

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16
Q

Asn

A

Asparagine

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17
Q

cys

A

Cysteine

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18
Q

Gln

A

Glutamine

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19
Q

Glu

A

Glutamic Acid

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20
Q

Gly

A

Glycine

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21
Q

His

A

Histidine

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22
Q

IIe

A

Isoleucine

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23
Q

Leu

A

Leucine

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24
Q

Lys

A

Lysine

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25
Q

Met

A

Methionine

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26
Q

Phe

A

Phenylalanine

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27
Q

Pro

A

Proline

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28
Q

Ser

A

Serine

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29
Q

Thr

A

Threonine

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30
Q

Trp

A

Tryptophan

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31
Q

Tyr

A

Tyrosine

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32
Q

Val

A

Valine

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33
Q

Sec

A

Selenocysteine

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34
Q

Pyl

A

Pyrrolysine

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35
Q

● Plays a role in cell division

A

Arginine

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35
Q

● Plays a role in cell division

A

Arginine

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36
Q

Healing of wounds, stimulation of protein synthesis
● Immune function

A

Arginine

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37
Q

Release of hormones

A

Arginine

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38
Q

Required for the generation of urea and synthesis of
creatin

A

Arginine

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39
Q

is the less toxic form produced from the
ammonia metabolized in the urea cycle

A

Urea

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40
Q

is a compound
involved in the supply of energy for muscle
contraction

A

Creatin

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41
Q

is synthesized with arginine

A

Creatine

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42
Q

when broken down forms creatinine

A

Creatinine

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43
Q

● Direct precursor of histamine

A

Histidine

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44
Q

● Repair body tissues

A

histidine

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45
Q

● Maintain myelin sheaths that protect the nerve cells

A

histidine

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46
Q

Helps manufacture RBC and WBC

A

histidine

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47
Q

● Protect the body from heavy metal toxicity

A

histidine

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48
Q

Needed for hemoglobin formation

A

Isoleucine

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49
Q

Helps to regulate blood and glucose levels and maintain
energy levels

A

Isoleucine

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50
Q

Boosts healing of muscle, skin, and bones

A

Leucine

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51
Q

Optimal growth of infants and for nitrogen balance in
adults

A

Leucine

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51
Q

● Lowers blood glucose levels

A

Leucine

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52
Q

Plays a role in the production of antibodies and
antibodies (immunoglobulins) and lowers triglyceride
levels

A

Lysine

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53
Q

Needed for proper growth and bone development in
children and to maintain a proper nitrogen balance in
adults

A

Lysine

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54
Q

Helps in the absorption of calcium and the formation of
collagen

A

Lysine

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55
Q

Helps initiate translation of messenger RNA

A

Methionine

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56
Q

First amino acid encoded during translation

A

Methionine

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57
Q

If __________is not encoded, translation won’t
happen

A

methionine

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58
Q

The codon that encodes for methionine is the
start codon, ________

A

AUG

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59
Q

Source sulfur

A

Methionine

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60
Q

functions for the normal metabolism and
growth of the body

A

sulfur - methionine

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61
Q

● Assist the breakdown of fats

A

methionine

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62
Q

● Helps to detoxify lead and other heavy metals

A

methionine

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63
Q

● Helps diminish muscle weakness

A

methionine

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64
Q

● Prevents brittle hair

A

methionine

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65
Q

Promotes alertness and vitality, elevates mood,
decreases pain, aids memory and learning

A

phenylalanine

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66
Q

● Used to treat arthritis and depression

A

phenylalanine

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67
Q

phenylalanine Used by brain to produce _______

A

norepinephrine

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68
Q

Uses active transport channel to cross the BBB

A

Phenylalanine

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69
Q

BBB

A

blood brain barrier

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70
Q

Interferes with the production of serotonin

A

phenylalanine

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71
Q

Part of the composition of aspartame

A

phenylalanine

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72
Q

Common sweetener in (?) food as sugar
replacment

A

aspartame

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73
Q

Important in the component in the formation of protein,
collagen, elastin, and tooth enamel

A

threonine

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74
Q

Helps maintain proper protein balance and aids in liver
function, metabolism, and assimilation

A

threonine

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75
Q

Precursor for serotonin (5-hydroxytryptamine) and
melatonin

A

trytophan

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76
Q

■ Stabilized the mood

A

Serotonin

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77
Q

■ Person feeling happy

A

Serotonin

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78
Q

Hormone secreted by pineal gland

A

melatonin

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79
Q

Sleep week cycle (highest during
night time

A

melatonin

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80
Q

● Natural relaxant

A

trytophan

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81
Q

Alleviate insomnia by inducing sleep, soothes anxiety
and reduces depression

A

trytophan

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82
Q

● Used in treatment of migraine headaches

A

trytophan

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83
Q

● Aids in weight control by reducing appetite

A

trytophan

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84
Q

● Helps control hyperactivity in children

A

trytophan

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85
Q

● Heaviest among all the amino acids

A

trytophan

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86
Q

Needed for muscle metabolism and coordination, tissue repair, maintenance of nitrogen balance

A

valine

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87
Q

● Used by muscle tissue as an energy source

A

valine

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88
Q

Used in treatments for muscle, mental and emotional
problems (insomnia, anxiety, liver and gallbladder
disease)

A

valine

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89
Q

Involved in the breakdown of glucose

A

Alanine

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90
Q

● Product of the breakdown of DNA

A

Alanine

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91
Q

● Transfer of nitrogen from the peripheral tissue to the liver

A

alanine

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92
Q

Helps in reducing the buildup of toxic substances that are
released into muscle

A

alanine

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93
Q

Strengthens the immune system through production of
antibodies

A

alanine

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94
Q

● First amino acid to be isolated

A

asparagine

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95
Q

● From asparagus juice

A

asparagine

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96
Q

Converting one amino acid into another via amination
and transamination

A

asparagine

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97
Q

Amine group is introduced to an
organic molecule

A

Amination

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98
Q

Amino acid is transferred to an alpha
keto acid (alpha ketoglutarate)

A

Transamination

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99
Q

Required by the nervous system and synthesis of
ammonia

A

Asparagine

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100
Q

A metabolite in the urea cycle and participates in
gluconeogenesis

A

Aspartic acid

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101
Q

● Named after cystine (precursor)

A

Cysteine

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102
Q

will travel in your cells, and as it goes
inside the cells, it will be reduced to 2 cysteine
molecules

A

cystine

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103
Q

● Also known as half-cystine residue

A

cysteine

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104
Q

● Production of flavors

A

cysteine

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105
Q

● Contains sulfur

A

cysteine

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106
Q

Serves as a neurotransmitter and dysregulation has been
linked to epileptic seizures

A

Glutamic acid

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107
Q

● aids in transporting potassium to the spinal fluid

A

Glutamic acid

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108
Q

● responsible for the taste umami

A

Glutamic acid

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109
Q

food additive/food enhancer(sodium salt, monosodium
glutamate (bitsin)

A

Glutamic acid

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110
Q

● most abundant amino acid in the body

A

Glutamine

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111
Q

assists in maintaining the proper acid/alkaline balance in
the body (regulates pH)

A

Glutamine

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112
Q

supplement used for muscle growth in weightlifting and
bodybuilding

A

Glutamine

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113
Q

transports ammonia to the liver

A

Glutamine

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114
Q

is toxic to the body (increased levels
is dangerous), may lead to comatose

A

ammonia

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115
Q

● Simplest amino acid

A

Glycine

116
Q

One element in the side chain

A

no stereoisomer

117
Q

only amino acid not optically active because it has no
stereoisomers

A

Glycine

118
Q

● has a sweet taste and is used as a sweetener

A

glycine

119
Q

● Inhibitory neurotransmitter in the cns

A

glycine

120
Q

helps in the synthesis of bile acids

A

glycine

121
Q

retards muscle degeneration, improves glycogen storage
and promotes healing

A

glycine

122
Q

precursor of hydroxyproline

A

Proline

123
Q

Technically not an amino acid, but an imino acid

A

proline

124
Q

role in wound healing and molecular recognition

A

Proline

125
Q

● works with vit. c to promote healthy connective tissues

A

Proline

126
Q

technically not a protein since it is an imino acid due to its
cyclic structure

A

proline

127
Q

needed for proper metabolism of fats and fatty acids

A

serine

128
Q

● highly concentrated in all cell membranes

A

serine

129
Q

● Component of the protective myelin sheaths surrounding
nerve fibers

A

serine

130
Q

precursor of epinephrine, norepinephrine, dopamine, t3
and t4

A

Tyrosine

131
Q

_______are thyroid hormones

A

Tyrosine

132
Q

● stimulates metabolism

A

Tyrosine

133
Q

mood elevator, suppresses appetite and helps reduce
body fat

A

tyrosine

134
Q

treatment of chronic fatigue, narcolepsy, anxiety,
depression, low sex drive, allergies and headaches

A

tyrosine

135
Q

TWO NEW AMINO ACIDS (established 2002

A

Selenocysteine
Pyrrolysine

136
Q

encoded by uga codon

A

selenocysteine

137
Q
  • a sulfur in cysteine is
    replaced by selenium
A

selenium analogue

138
Q

● found in some enzymes

A

Formate dehydrogenase
○ Glycine reductase
○ And some hydrogenases

139
Q

main bile acid in the body:

A

folic acid and chenodeoxycholic acid

139
Q

main bile acid in the body:

A

folic acid and chenodeoxycholic acid

140
Q

Encoded by UAG codon

A

Pyrrolysine

141
Q

● Used by archaea and unicellular organisms

A

Pyrrolysine

142
Q

product of ketogenesis

A

acetoacetyl coa and Acetyl coa

143
Q

Can be
(?) in the metabolic pathway
ketogenesis

A

Acetoacetyl coa

144
Q

can enter
ketogenesis or will be
allowed to enter the citric
acid cycle

A

acetyl coa

145
Q

Can generate precursor of glucose:
Pyruvate→ gluconeogenesis or
create Acetyl CoA and enter citric
acid cycle

A

Glucogenic

146
Q

○ Process of removing amino group

A

● Oxidative deamination or Transamination

147
Q

alpha keto glutamate
● Will enter common
metabolic pathway

A

keto acid

148
Q

Toxic to the body and should
be converted to less toxic
form

A

UREA

149
Q

Toxic to the body and should
be converted to less toxic
form

A

Ammonia

150
Q

Rare, inherited disorders of aminoacid metabolism

A

AMINOACIDOPATHIES

151
Q

Abnormalities in activity of a specific enzyme in the
metabolic pathway

A

AMINOACIDOPATHIES

152
Q

Abnormalities in the membrane transport system for
amino acids

A

AMINOACIDOPATHIES

153
Q

● Brought about by genetic defect.

A

AMINOACIDOPATHIES

154
Q

● autosomal recessive trait

A

PHENYLKETONURIA (PKU)

155
Q

Must inherit 2 mutated gene one from each
parent

A

PHENYLKETONURIA (PKU)

156
Q

● Total absence of activity of PHENYLALANINE

A

PHENYLKETONURIA (PKU)

157
Q

Catalyzes the conversion of phenylalanine to
tyrosine

A

HYDROXYLASE

158
Q

if there’s accumulation in the blood

A

hyperphenylalaninemia

159
Q

If the phenylalanine is present in the urine

A

phenylketonuria

160
Q

Occurs as a result of the toxic effects of the
brain of phenylpyruvate or one of its metabolic
by-products

A

Retarded mental development - 2nd or 3rd week of life - expect microcephaly

161
Q

deamination of
phenylalanine

A

Phenylpyruvate

162
Q

decarboxylation and
oxidation of phenylpyruvate

A

Phenylacetic acid

163
Q

glutamine conjugate
of phenylacetate

A

Phenylacetylglutamine

164
Q

If the mother has phenylketonuria and the baby kay wala,
maagapan mo na ma experience ng baby ang
phenylketonuria

A

Make sure that the mother will
undergo phenylalanine restricted diet

165
Q

Spores of Bacillus subtilis are
incorporated into an agar plate that
contains beta-2- thienylalanine
(antagonist)

A

Guthrie Bacterial
Inhibition
Assay

166
Q

● Filter paper disk impregnated with
blood from the infant is placed on the
agar mg/dL, phenylalanine counteracts the
antagonist and bacterial growth
occurs

A

Guthrie Bacterial
Inhibition
Assay

167
Q

if may bacterial
growth around the disc

A

Positive

168
Q

if walang growth

A

Negative

169
Q

Allow the extract to react with the
microtiter plate which contains
ninhydrin, succinate, leucylalanine,
and copper tartrat

A

Microfluorometric
assay

170
Q

direct measurement of phenylalanine
in dried blood filter disks

A

Microfluorometric
assay

171
Q

Based on the fluorescence of a
complex formed of
phenylalanine-ninhydrin-copper in
the presence of a dipeptide
(Lleucyl-L-alanine

A

Microfluorometric
assay

172
Q

● Excitation/emission wavelengths of
360 nm and 530 nm respectively

A

Microfluorometric
assay

173
Q

Positive blood test results: bacterial halo =

A

PKU

174
Q

Negative controls

A

no bacterial growth

175
Q

Positive controls

A

increasing phenylalanine

176
Q

Reference method/standard method

A

High-Performance Liquid Chromatography (HPLC)

177
Q

is one of the diseases that is tested in
newborn screening

A

PKU

178
Q

monitoring

A

Urine test

179
Q

nvolves the reaction of ferric chloride with
phenylpyruvic acid (possible analyte present)
in urine to produce a

A

green color

180
Q

Involves the reaction of ferric chloride with
phenylpyruvic acid (possible analyte present)
in urine to produce a green color

A

Reagent strip test

181
Q

Characterized by excretion of tyrosine and tyrosine
catabolites in urine

A

Tyrosinemia

182
Q

■ Most severe
■ Possible symptoms: failure to thrive

A

Fumarylacetoacetate (FAA) hydrolase (type I)

183
Q

new born in HPLC

A

1.2 – 3.4 mg/dL (70-200 umol/L)

184
Q

scarring of liver tissue

A

Cirrhosis

185
Q

Autosomal recessive disorder

A

Alkaptonuria

186
Q

an arthritis-like degeneration

A

Ochronosis

187
Q

Also tested in newborn screen

A

Maple Syrup Urine Disease

188
Q

Autosomal recessive genetic disorder

A

Maple Syrup Urine Disease

189
Q

Maple syrup urine disease : Blocking the normal metabolism of

A

Leu, Ile and
Val

190
Q

Maple syrup urine disease: Modified Guthrie test:

A

4-azaleucine

191
Q

MPSUD : Microfluorometric assay

A

Leucine dehydrogenase above
4 mg/dL is indicative of MSUD

192
Q

Complications of MSUD

A

lethargy, failure to thrive, muscle rigidity, respiratory irregularities, mental retardation, comvulsions, acidosis, hypoglycemia

193
Q

Deficiency of isovaleryl-CoA dehydrogenase in leucine
pathway

A

Isovaleric Acidemia

194
Q

“sweaty feet” odor

A

Isovaleric acidemia

195
Q

● Perform chromatography

A

Isovaleric acidemia

196
Q

Increased levels of homocysteine

A

Homocystinuria

197
Q

Intermediate amino acid in the synthesis of
cysteine from methionine

A

Homocysteine

198
Q

Impaired activity of cystathionine beta-synthase
(homocysteine to cysteine)

A

homocystinuria

199
Q

Cysteine and homocysteine are reduced by
sodium cyanide to free-thiol

A

● Cyanide-Nitroprusside Urine Spot Test

200
Q

Results from inherited enzyme deficiencies in the urea
cycle

A

Citrullinemia

201
Q

○ Then, reacted to sodium nitroprusside to
produce a red-purple colo

A

Cyanide-Nitroprusside Urine Spot Test

202
Q

Silver nitrate reduces homocysteine
to form reddish color

A

Silver-nitroprusside Test

203
Q

COMPLICATIONS OF SILVER NITROPRUSSIDE TEST

A

COMPLICATIONS:
○ Thromboembolism, Cardiovascular risk,
Atherosclerotic disease, Low folate
concentrations, Vitamin B12 deficienc

204
Q

lack of the enzyme argininosuccinic acid
synthetase (ASS)

A

type 1 OF CITRULLINEMIA

205
Q

caused by a mutation of the gene that would
provide instructions for making the protein citrin

A

Type 2

206
Q

helps transport molecules inside
cells that used to produce simple
sugars, proteins, nucleotides, and
molecules used in the urea cycle

A

citrin

207
Q

Citrullinemia complications

A

Vomiting, high ammonia levels and
Mental retardation may lead to comatose

208
Q

Results from inherited enzyme deficiencies in the urea
cycle

A

Argininosuccinic Aciduria

209
Q

● Deficiency in argininosuccinate lyase (ASL)

A

Argininosuccinic aciduria

210
Q

a defect in the amino acid transport system rather than a
metabolic enzyme deficiency

A

Cystinuria

211
Q

■ Insoluble
■ Tends to precipitate in the kidney
tubules

A

Cystinuria

212
Q

Aromatic odor

A

normal

213
Q

Foul, ammonia-like odor

A

bacterial decomposition, urinary tract infection

214
Q

Fruity, sweet

A

ketones (diabetes mellitus, salvation, vomitting)
k - DSV

215
Q

Maple syrup

A

Maple syrup urine disease

216
Q

Mousy

A

Phenylketonuria

217
Q

Rancid

A

tyrosinemia

218
Q

Sweaty feet

A

Isovaleric acidemia

219
Q

Cabbage

A

Methionine malabsorption

220
Q

Bleach

A

Contamination

221
Q

The group that is free is called

A

Carboxyl group

222
Q

● Covalently linked polymers of amino acids

A

PROTEINS

223
Q

Give me the primary structure of proteins

A

A. primary structure
B. Secondary structure
C. tertiary structure
D. Quarternary structure

224
Q

The different amino acids that compose a
specific protein in a linear wa

A

Primary structure

225
Q

The peptide chains are folded regularly which
forms

A

Secondary structure
- alpha helix and beta pleated sheets

226
Q

Folded secondary structure into a 3D form
○ Considered a polypeptide

A

Tertiary structure

227
Q

Combined tertiary polypeptide structure with
other polypeptide

A

Quaternary Structure

228
Q

The mRNA is partnered with an anti-codon with
the help of the ribosomal complex

A

Translation

229
Q

○ Purely made up of amino acids

A

Simple

230
Q

Contain peptide chains on hydrolysis yield only
amino acids

A

simple

231
Q

Not entirely made up of amino acids only

A

conjugated

232
Q

Comprise a protein (apoprotein) and a
nonprotein moiety (prosthetic group)

A

conjugated

233
Q

Conjugated sample

A

Lipids (lipoprotein), CHO
(glycoprotein), porphyrins
(hemoglobin), metals (ceruloplasmin)

234
Q

Simple sample

A

albumin

235
Q

Classification of Proteins (Function)
(9)

A

enzymes
hormones
transport protein
Immunoglobulins (Antibodies)
Structural proteins
Storage proteins
energy source
Osmotic force
Blood coagulation

236
Q

Catalyze chemical reactions

A

Enzymes

237
Q

Control action of specific cells or organs

A

Hormones

238
Q

Move substance inside the body

A

transport proteins

239
Q

○ Gives protection against foreign objects

A

Immunoglobulins (antibodies)

240
Q

○ Components of cells and tissues

A

● Structural proteins

241
Q

○ Acts as reserves

A

● Storage proteins

242
Q

Capable of affecting the distribution of water in
the body

A

osmotic force

243
Q

Clotting factors - fibrinogen

A

Blood coagulation

244
Q

FIVE FRACTIONS OF PLASMA PROTEINS

A

Albumin, A1 globulins, A2 Globulins , B globulins, Y globulins,

245
Q

α1-fetoprotein
○ α-antitrypsin
○ HDL

A

A 1 globulin

246
Q

haptoglobin
○ ceruloplasmin
○ α2-macroglobulin

A

A2 globulin

247
Q

○ transferrin
○ C-reactive protein

A

B globulin

248
Q

Immunoglobulins

A

Y globulin

249
Q

● Also known as transthyretin

A

PREALBUMIN

250
Q

● Migrates ahead of albumin

A

pre-albumin

251
Q

Transport protein of thyroid hormones T 3 and T4

A

Triiodothyronine and thyroxine - pre albumin

252
Q

Binds with retinol-binding protein to form a complex that
transports retinol (vitamin A)

A

PREALBUMIN

253
Q

● Rich in tryptophan

A

pre-albumin

254
Q

Hepatic damage

A

Decrease prealbumin

255
Q

Acute phase inflammatory response

A

Decrease prealbumin

256
Q

Tissue necrosis

A

● Decrease prealbumin

257
Q

Sensitive marker of poor protein nutritional
status

A

Decrease prealbumin

258
Q

● Present in highest concentration

A

ALBUMIN

259
Q

Increase in prealbumin

A

Steroids, alcoholism and chronic renal failure
SAC

260
Q

Albumin in the body can maintain the
appropriate fluid balance in our body
■ Regulating colloid osmotic pressure of
the intravascular fluid

A

○ Colloid osmotic pressure

261
Q

○ Transcapillary escape rate

A

Rate of movement of albumin leaving
the blood circulation

262
Q

Can bind to thyroid hormones
■ Similar to pre albumin

A

bind to othersubstance

263
Q

Can bind to conjugated bilirubin, iron,
calcium and magnesium

A

ALBUMIN

264
Q

Resulting in the inability of hepatocytes to
synthesize albumin

A

hypoalbuminemia - liver disease

265
Q

Inflammation and intestinal mucosal disease.
○ The interstitial fluid that contains albumin leaks
out in the intestine and will be easily excreted
esp. The person is suffering from diarrhea

A

Hypoalbuminemia - gastrointestinal loss

266
Q

Kidney can’t function properly and cannot filter
all proteins → proteins will go out from the
blood circulation→ urine

A

Loss in the urine in renal disease.

267
Q

Seen in dehydration

A

hyperalbuminemia

268
Q

● Absence of albumin

A

analbuminemia

269
Q

Bakante ang albumin (lower left)

A

anaalbuminemia

270
Q

Unusual molecular characteristics

A

Bisalbuminemia

271
Q

Genetic in origin resulting from an autosomal recessive
trait

A

bisalbuminemia

272
Q

● condition of having two types of serum albumin that differ
in mobility during electrophoresis

A

Bisalbuminemia

273
Q

Consists of alpha1, alpha2, beta, and gamma fractions in
electrophoresis

A

Globulins

274
Q

● Acute-phase reactant

A

ALPHA 1 - ANTITRYPSIN

275
Q

Neutralize trypsin-like enzyme that can cause hydrolytic
damage to structural protein

A

ALPHA 1 - ANTITRYPSIN

276
Q

Alpha 1 antitrypsin increase

A

Increased: inflammation, pregnancy, contraceptive use

277
Q

Alpha 1 antotrypsin decrease

A

Deficiency: Severe, degenerative, emphysematous
pulmonary disease

278
Q

Synthesized initially by the fetal yolk sac and then by the
parenchymal cells of the live

A

ALPHA 1 - FETOPROTEIN (AFP)

279
Q

13 weeks’ gestation

A

Peak:

280
Q

34 week’s gestation

A

Recede

281
Q

Incomplete closure of embryonic
neural tube

A

Spina bifida and neural tube defects

282
Q

Incomplete spinal cord

A

Spina bifida and neural tube defects

283
Q

Narrowing or absence of a portion of
the intestine of the fetus

A

○ Atresia of the gastrointestinal tract

284
Q

Not well; excessively fatigue

A

○ Fetal distress

285
Q

Immunodeficiency disorder

A

○ Ataxia-telangiectasia

286
Q

Increased level of tyrosine

A

tyrosinosis

287
Q

Anti-D of the mother attacks the RBC
with the D antigen of the fetus

A

Hemolytic disease of the newborn (HDN)

288
Q

Hepatolenticular degeneration
■ Autosomal recessive inherited
disease

A

○ Wilson’s disease

289
Q

Kinky hair disease
■ There is a problem in the absorption
of copper. Ceruloplasmin is not only a
carrier of copper it also contains
copper. If the body has a problem in
the level of copper, then definitely the
ceruloplasmin will be directly affecte

A

menke’s syndrome / kinyky’s hair disease

CLIN CHEM LEC (13 decks)

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