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CLINICAL CHEMISTRY > Amino Acids and Proteins > Flashcards

Amino Acids and Proteins Flashcards

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1
Q

Class of inherited errors of metabolism in which there is an enzyme defect that inhibits the body’s ability to metabolize certain amino acids

A

Aminoacidopathies

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2
Q

Cause of phenylketonuria

A

Phenylalanine hydroxylase (PAH)
deficiency

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3
Q

Urine odor of patient with phenylketonuria

A

Musty/Mousy odor

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4
Q

Patients with PKU may experience

A

Mental retardation
Microcephaly

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5
Q

A co-factor in the enzymatic hydroxylation of phenylalanine, tryptophan, and tyrosine

A

Tetrahydrobiopterin

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6
Q

Non-protein chemical/entity that must bind to a particular enzyme before a reaction occurs

A

Co-factor

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7
Q

Allows early detection IEM and early implementation of the treatment

A

Newborn screening test

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8
Q

Goal of PKU treatment

A

Maintain blood level of phenylalanine (2-10 mg/dL or 120- 160 μmol/L)

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9
Q

First drug to manage PKU

A

Kuvan (sapropterin dihydrochloride)

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10
Q

Positive result of Ferric Chloride Tube Test for PKU

A

Permanent blue-green color

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11
Q

Positive result of Guthrie Bacterial Inhibition Test for PKU

A

Bacterial growth

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12
Q

Inhibitor of B. subtilis

A

B-2-thienylalanine

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13
Q

Reference method for quantitative serum phenylalanine

A

High-Performance Liquid Chromatography (HPLC)

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14
Q

Used in screening for inherited disorders in newborns

A

Tandem Mass Spectrometry (MS/MS)

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15
Q

Characterized by the excretion of tyrosine and tyrosine catabolites in urine

A

Tyrosinemia

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16
Q

Cause of type 1 tyrosinemia

A

Fumarylacetoacetate hydrolase deficiency

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17
Q

Most severe form of tyrosinemia

A

Type 1

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18
Q

Cause of type 2 tyrosinemia

A

Tyrosine aminotransferase deficiency

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19
Q

Cause of type 3 tyrosinemia

A

4-hydroxyphenylpyruvate dioxygenase or p-hydroxyphenylpyruvic acid dioxygenase deficiency

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20
Q

Positive result of Ferric chloride tube test for tyrosinemia

A

Transient green color

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21
Q

Positive result of Nitroso-naphthol test for tyrosinemia

A

Orange-red color

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22
Q

Drug to treat tyrosinemia

A

Nitrisinone

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23
Q

Cause of alkaptonuria

A

Homogentisate oxidase deficiency

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24
Q

Urine color of patient with alkaptonuria

A

Brownish-black after exposure to air

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25
Q

Positive result of Ferric chloride tube test for alkaptonuria

A

Deep blue/black

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26
Q

Positive result of Clinitest for alkaptonuria

A

Yellow precipitate

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27
Q

Positive result of Homogentisic acid test for alkaptonuria

A

Black

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28
Q

Treatment for alkaptonuria

A

Vitamin C

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29
Q

Cause of MSUD

A

α-ketoacid decarboxylase deficiency or defect

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30
Q

MSUD blocks the normal metabolism of the three essential branched-chain amino acids: _____, _____, _____

A

Leucine
Isoleucine
Valine

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31
Q

Urine odor of patient with MSUD

A

Maple syrup or burnt sugar odor

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32
Q

Positive result of 2,4-dinitrophenylhydrazine (DNPH) test for MSUD

A

Yellow precipitate or turbidity

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33
Q

Cause of isovaleric acidemia

A

Isovaleryl-CoA dehydrogenase deficiency

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34
Q

Urine odor of patients with isovaleric acidemia

A

Sweaty feet odor, due to build-up of isovaleric acid

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35
Q

Positive result of p-Nitroaniline Test for isovaleric acidemia

A

Emerald green

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36
Q

Cause of homocystinuria

A

Cystathionine β-synthase deficiency

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37
Q

Positive result of Cyanide-nitroprusside test for homocystinuria

A

Red-purple color

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38
Q

Positive result of Silver-nitroprusside test for homocystinuria

A

Red-purple color

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39
Q

Class of genetic diseases called urea cycle disorders

A

Citrullinemmia

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40
Q

Types of citrullinemia

A

TYPE 1: the most common form, lack of the enzyme argininosuccinic acid synthetase (buildup of citrulline and ammonia in the blood)

TYPE 2: caused by a mutation of the gene that makes the protein citrin

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41
Q

Cause of arginosuccinic aciduria

A

Argininosuccinic acid lyase deficiency

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42
Q

Positive result of Cyanide-Nitroprusside Test for Cystine

A

Red-purple

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43
Q

Blood samples for amino acid analysis should be drawn after

A

At least a 6-8 hour fast

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44
Q

Tube and additive used in samples for amino acid analysis

A

Heparin; green tube

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45
Q

Deproteinization should be performed within _____ of sample collection and analysis should be performed _____

A

30 minutes
Immediately

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46
Q

In cases that a sample cannot be analyzed immediately, the sample should be

A

Frozen at −20°C to −40°C

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47
Q

Urinary amino acid analysis can be performed on random specimens. True or False?

A

True

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48
Q

Urine preservative for protein analyses

A

Thymol

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49
Q

Method of choice for screening test of amino acids

A

Thin-layer chromatography

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50
Q

A process that allows the separation of ion and molecules base on affinity to ion exchangers

A

Ion exchange chromatography/ Ion chromatography

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51
Q

Possess negatively charged group and attract positively charged ion

A

Cationic exchangers

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52
Q

Possess positively charged group and attract negatively charged ion

A

Anionic exchangers

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53
Q

Separates ions base on electrophoretic mobility
with the use of applied voltage

A

Capillary electrophoresis

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54
Q

Technique use to break down selected ions/precursor ions into fragments or product ions (fragments reveal the aspect of the ion)

A

MS/MS (tandem mass spectrophotometry)

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55
Q

Are polymers of amino acids that are linked covalently through peptide bonds

A

Proteins

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56
Q

Protein are micromolecules. True or False?

A

False; macromolecules

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57
Q

All proteins are synthesized in the liver. True or False?

A

False; except immunoglobulins (plasma cells)

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58
Q

Atoms in protein compound

A

Carbon
Oxygen
Hydrogen
Nitrogen
Sulfur

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59
Q

4 structures of protein

A

Primary
Secondary
Tertiary
Quaternary

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60
Q

Linear sequence of amino acids

A

Primary structure

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61
Q

Protein structure that determines the identity of protein

A

Primary structure

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62
Q

Specific regular three-dimensional conformations into which portions of the polypeptide chain fold (α-helix; β-pleated sheets; bend conformation)

A

Secondary structure

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62
Q

Protein structure which adds new property such as strength and flexibility due to polypeptide chain fold

A

Secondary structure

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63
Q

Actual three-dimensional structure or folding pattern of the protein

A

Tertiary structure

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64
Q

Refers to overall shape and formation of protein

A

Tertiary structure

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65
Q

Protein structure with spatial relationship to one another

A

Tertiary structure

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66
Q

The shape or structure that results from the interaction of more than one protein molecule, or protein subunits

A

Quaternary structure

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67
Q

Most abundant protein in the body

A

Collagen

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68
Q

Process where protein loose its shape and functions

A

Denaturation

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69
Q

Causes of protein denaturation

A

Heat
Hydrolysis
Strong acids
Alkali
Enzymatic reaction
Exposure to urea
UV light

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70
Q

Classification of proteins by function

A

Enzymes
Hormones
Transport proteins
Immunoglobulins
Structural proteins
Storage proteins
Energy source
Osmotic source

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71
Q

Catalyze chemical reactions

A

Enzymes

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72
Q

Chemical messengers that control action of specific organ or system

A

Hormones

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73
Q

Transport movement of ions, small molecules, or macromolecules

A

Transport proteins

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74
Q

Mediate the humoral immune response

A

Immunoglobulins

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75
Q

The only protein not produced by the liver

A

Immunoglobulins

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76
Q

Proteins for structures of cells and tissues

A

Structural proteins

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77
Q

Protein that serve as reserves of metal ions and amino acids

A

Storage proteins

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78
Q

Protein for tissues and muscles

A

Energy source proteins

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79
Q

Function in the distribution of water throughout the compartments of the body

A

Osmotic force proteins

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80
Q

Example of osmotic force proteins

A

Albumin (important in colloid osmotic pressure)

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81
Q

Structural Classification of Proteins (SCOP) database

A

Class
Fold
Superfamily
Family

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82
Q

Families of Structurally Similar Proteins (FSSP) / Fold Classification is based on

A

Three-dimensional structure of proteins

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83
Q

Protein that contains peptide chains of only amino acids

A

Simple Proteins

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84
Q

Examples of globular proteins

A

Albumin
Hemoglobin

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85
Q

Examples of fibrous proteins

A

Troponin
Collagen

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86
Q

Consist of a protein and a non-protein (prosthetic) group

A

Conjugated Proteins

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87
Q

Metals + Proteins

A

Metalloproteins

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88
Q

Examples of metalloproteins

A

Ferritin
Ceruloplasmin

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89
Q

Lipids + Proteins

A

Lipoproteins

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90
Q

Examples of lipoproteins

A

High Density Lipoprotein
Low Density Lipoprotein
Very Low-Density Lipoprotein
Chylomicrons

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91
Q

Carbohydrates + Protein (10-40% Carbs)

A

Glycoproteins

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92
Q

Examples of glycoproteins

A

Haptoglobin
Alpha-1 antitrypsin

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93
Q

Carbohydrates + Proteins (>40% of Carbs)

A

Mucoproteins

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94
Q

Chromatin – DNA + Histones

A

Nucleoproteins

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95
Q

The most frequently analyzed of all the proteins

A

Plasma proteins

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96
Q

Two groups of plasma proteins

A

Albumin

Globulin
Alpha-1
Alpha-2
Beta
Gamma

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97
Q

Migrates before albumin in a classic electrophoresis

A

Prealbumin (Transthyretin)

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98
Q

The transport protein for thyroxine (T4) and triiodothyronine (T3) (thyroid hormones)

A

Prealbumin

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99
Q

Binds with retinol-binding protein (Vitamin A)

A

Prealbumin

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100
Q

Causes of decreased prealbumin

A

Hepatic Damage
Acute-phase inflammatory response
Tissue necrosis

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101
Q

Causes of increased prealbumin

A

Alcoholism
Steroid medication
Chronic Renal failure

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102
Q

Sensitive marker of nutritional status

A

Prealbumin

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103
Q

In terms of nutritional status, a decrease in prealbumin indicates

A

Poor nutrition

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104
Q

Most abundant protein in plasma

A

Albumin

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105
Q

Responsible for nearly 80% of the colloid osmotic pressure (COP) of the intravascular fluid

A

Albumin

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106
Q

Osmotic pressure exerted by large molecules like albumin which helps fluid stay within the instead of leaking into tissues

A

Colloid Osmotic Pressure

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107
Q

Concentration of this protein decreases during inflammation

A

Negative acute-phase reactant protein

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108
Q

Causes of decreased albumin

A

Malnutrition and malabsorption
Liver disease
Protein-losing enteropathy or gastrointestinal loss
Renal disease
Burns or exfoliative dermatitis
Hypothyroidism
Polydipsia or excess administration of IV fluid
Mutation causing analbuminemia or bisalbuminemia
Sepsis

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109
Q

Causes of increased albumin

A

Dehydration
After excessive albumin infusion

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110
Q

Albumin with unusual molecular
characteristics

A

Bisalbuminemia

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111
Q

Increased vascular permeability in the capillary

A

Sepsis

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112
Q

Cause of α1-antitrypsin deficiency

A

Mutations in the SERPINA1 gene [Serine Protease Inhibitor (SERPIN) Family A Member 1]

113
Q

Provides information for a-1
Antitrypsin synthesis

A

SERPINA1

114
Q

Concentration increases during inflammation

A

Acute-phase reactant

115
Q

Causes of increased a1-antitrypsin

A

Inflammatory reactions
Pregnancy
Contraceptive use

116
Q

Sites for A1-Antitrypsin synthesis

A

Human Amniotic epithelial cells
Liver

117
Q

Major component of a1-globulin fraction

A

a1-antitrypsin

118
Q

Binds the hormone estradiol (normal fetuses)

A

a1-Fetoprotein (AFP)

119
Q

a1-Fetoprotein (AFP) is produced by

A

Developing embryo and fetus
Parenchymal cells of the liver

120
Q

a1-Fetoprotein (AFP) increases after birth. True or False?

A

False; decreases

121
Q

Protects the fetus from immunologic attack by the mother

A

a1-Fetoprotein (AFP)

122
Q

Causes of increased a1-Fetoprotein (AFP)

A

Neural tube defects (spina bifida and anencephaly)
Abdominal wall defects
Fetal distress

123
Q

Causes of decreased a1-Fetoprotein (AFP)

A

Down syndrome (Trisomy 21)
Edward’s Syndrome (Trisomy 18)

124
Q

a1-Acid Glycoprotein (Orosomucoid) is a negative acute-phase reactant. True or False?

A

False; acute-phase reactant

125
Q

Causes of increased a1-Acid Glycoprotein (Orosomucoid)

A

Stress
Inflammation
Tissue damage
Acute myocardial infarction (AMI)
Trauma
Pregnancy
Cancer
Pneumonia
Rheumatoid arthritis
Surgery

126
Q

Serine proteinase inhibitor

A

α1-Antichymotrypsin

127
Q

Cause of increased α1-Antichymotrypsin

A

Inflammation

128
Q

Cause of decreased α1-Antichymotrypsin

A

Liver disease

129
Q

Mutations in α1-Antichymotrypsin production may lead to

A

Parkinson’s disease
COPD
Alzheimer’s disease (amyloid deposits)

130
Q

Play a role in inflammation and carcinogenesis

A

Inter-α-Trypsin Inhibitors

131
Q

Cause of increased Inter-α-Trypsin Inhibitors

A

Inflammatory disorders

132
Q

Major carrier protein of vitamin D and its metabolites in the VV (In VIVO)

A

Gc-Globulin (Group-Specific Component; Vitamin D–Binding Protein)

133
Q

Causes of decreased Gc-Globulin

A

Severe liver disease
Protein-losing syndromes

134
Q

Bind free hemoglobin to prevent the loss of hemoglobin and its constituent, iron

A

Haptoglobin

135
Q

Used to evaluate degree of intravascular hemolysis (HTR and HDN)

A

Haptoglobin

136
Q

Causes of increased Haptoglobin

A

Inflammatory diseases
Burns
Nephrotic syndrome

137
Q

Cause of decreased Haptoglobin

A

Hemolytic anemia

138
Q

Symptoms of Nephrotic syndrome

A

Massive proteinuria
Hypoalbuminemia
Hyperlipidemia

139
Q

Occurs due to the mismatch or incompatibility of a patient with the donor products

A

Hemolytic Transfusion Reaction (HTR)

140
Q

Occurs when the mother is Rh negative and has a baby who is Rh positive

A

Hemolytic Disease of the Newborn (HDN)

141
Q

Given to mothers who is Rh negative around 28 weeks of pregnancy

A

RhoGAM / Rh immunoglobulin

142
Q

Copper-containing α2-glycoprotein

A

Ceruloplasmin

143
Q

90% of copper is bound to _____; 10% is bound to _____

A

Ceruloplasmin
Albumin

144
Q

Causes of increased Ceruloplasmin

A

Inflammation
Cancers
Pregnancy

145
Q

Causes of decreased Ceruloplasmin

A

Wilson’s disease
Malnutrition
Malabsorption
Severe liver disease
Nephrotic syndrome
Menkes syndrome (kinky hair disease)

146
Q

Used to diagnose Wilson’s disease

A

Kayser-Fleischer rings in cornea

147
Q

Autosomal recessive inherited disorder associated with decrease levels of the protein ceruloplasmin and a subsequent increase in copper causing it to accumulate in liver, brain and other organs

A

Wilson’s disease

148
Q

Major component of the α2 band

A

a2-Macroglobulin

149
Q

Functions of a2-Macroglobulin

A

Inhibits proteases such as trypsin, thrombin, kallikrein, and plasmin

150
Q

Proteolytic enzyme that functions in the digestion of protein

A

Trypsin

151
Q

Enzymes that play a role in the coagulation system

A

Thrombin
Kallikrein
Plasmin

152
Q

Causes of increased a2-Macroglobulin

A

Nephrosis
Diabetes and liver disease

153
Q

Indicates the amount of iron in the body

A

Transferrin (Siderophilin)

154
Q

Causes of increased Transferrin (Siderophilin)

A

Liver disease
Malnutrition
Nephrotic syndrome

155
Q

Causes of decreased Transferrin (Siderophilin)

A

Iron Deficiency Anemia (IDA)
Hemochromatosis (bronze skin) or Bronze Diabetes

156
Q

Most prevalent nutritional deficit in the world

A

Iron Deficiency Anemia (IDA)

157
Q

Major component of the β-globulin fraction

A

Transferrin (Siderophilin)

158
Q

Function of Transferrin (Siderophilin)

A

Transport of iron and the prevention of loss of iron through the kidney

159
Q

Organ that synthesize transferrin

A

Liver

160
Q

Indication of high levels of transferrin

A

Signifies low iron which means there is less iron bound to transferrin
Iron Deficiency

161
Q

Binds heme released by hemoglobin degradation and the complex is carried to the liver where it is destroyed

A

Hemopexin

162
Q

Causes of increased Hemopexin

A

Inflammation
Diabetes mellitus
Duchenne type muscular dystrophy
Some malignancies

163
Q

Causes of decreased Hemopexin

A

Hemolytic anemia or intravascular hemolytic anemia

164
Q

Progressive muscle degeneration in weakness due to the alteration in the protein dystrophin that helps keep muscle intact

A

Duchenne type muscular dystrophy

165
Q

Protein that is essential in muscular contractions

A

Dystrophin

166
Q

Serum hemopexin level reflects how much heme is present in the blood, therefore, a low hemopexin level indicates decreased degradation of heme containing compounds. True or False?

A

False; significant degradation of heme containing compounds

167
Q

Transport cholesterol, triglycerides, and phospholipids in the blood

A

Lipoproteins

168
Q

The light chain component of the major histocompatibility complex

A

β2-Microglobulin

169
Q

Function of Major Histocompatibility Complex (MHC)

A

Bind peptide fragments derived from pathogens and display them on the cell surface ready for recognition by appropriate T-lymphocytes

170
Q

Causes of increased β2-Microglobulin

A

Rheumatoid arthritis
Systemic lupus erythematosus
HIV

171
Q

Group of proteins that help your immune system to fight infection, heal injury and kill bacteria and viruses

A

Complement system

172
Q

The most abundant complement in serum

A

C3

173
Q

Cause of increased complement

A

Inflammatory conditions

174
Q

Causes of decreased complement

A

Malnutrition
Hemolytic anemia

175
Q

CD affected in Paroxysmal Nocturnal
Hemoglobinuria (PNH)

A

CD59
CD55

176
Q

Form a fibrin clot when activated by thrombin

A

Fibrinogen

177
Q

One of the largest proteins in blood plasma

A

Fibrinogen

178
Q

Causes of increased fibrinogen

A

Inflammatory disorders
Pregnancy
Oral contraceptives

179
Q

Cause of decreased fibrinogen

A

Extensive coagulation

180
Q

One of the first acute-phase reactant proteins to rise in response to inflammatory disorders

A

C-Reactive Protein (CRP)

181
Q

Causes of increased C-Reactive Protein (CRP)

A

Acute rheumatic fever
Bacterial infections
Myocardial infarctions
Rheumatoid arthritis
Carcinomatosis
Gout
Viral infections

182
Q

Glycoproteins composed of 82% to 96% protein and 4% to 18% carbohydrate produced by white blood cells, known as B cells, that confer humoral immunity

A

Immunoglobulins (Antibodies or Igs)

183
Q

Humoral immunity is otherwise known as

A

Antibody-mediated immunity

184
Q

5 classes of Immunoglobulins

A

IgG
IgA
IgM
IgD
IgE

185
Q

The most abundant class of antibodies found in blood plasma and lymph

A

IgG

186
Q

The main immunoglobulin found in mucous secretions (including tears, saliva, colostrum, vaginal fluid, etc.)

A

IgA

187
Q

The first antibody that appears in response to antigenic stimulation

A

IgM

188
Q

Antibody molecules that are present on the surface of most B cells

A

IgD

189
Q

Antibody associated with allergic and anaphylactic reactions

A

IgE

190
Q

The primary oxygen-carrying protein in striated and cardiac muscle

A

Myoglobin

191
Q

Myoglobin is a cardiac biomarker. True or False?

A

True

192
Q

Causes of increased myoglobin

A

AMI
Progressive muscular dystrophy
Crushing injury
Renal failure

193
Q

Myoglobin is cardiac specific. True or False?

A

False; not cardiac specific

194
Q

Cardiac troponins include

A

Troponin I (cTnI)
Troponin T (cTnT)

195
Q

The “gold standard” in the diagnosis of acute coronary syndrome

A

Cardiac troponin

196
Q

Blood supplied to the heart is suddenly blocked like in heart attack or myocardial infarction

A

Acute coronary syndrome (ACS)

197
Q

Specific for myocardial damage

A

Cardiac Troponin

198
Q

These are neurohormones that affect body fluid homeostasis and blood pressure

A

Brain natriuretic peptide or N-terminal brain natriuretic peptide

199
Q

Neurohormones are anti hypertensive agents which functions to decrease blood pressure. True or False?

A

True

200
Q

How does neurohormones affect fluid homeostasis?

A

Natriuresis
Diuresis

201
Q

Refers to increased urinary sodium excretion

A

Natriuresis

202
Q

Refers to increased urine excretion

A

Diuresis

203
Q

Function of neurohormone in the maintenance of blood pressure

A

Decreasing angiotensin II
Inhibiting production of norepinephrine

204
Q

Popular markers for congestive heart failure

A

Cardiac troponin

205
Q

Glycoprotein used to help predict the short-term risk of premature delivery

A

Fetal fibronectin (fFN)

206
Q

Amino acid fat hormone produced by adipocytes

A

Adiponectin

207
Q

Causes of decreased adiponectin

A

Heart disease
Type 2 diabetes
Metabolic syndrome
Obesity

208
Q

Correlation between adiponectin and body mass index (BMI)

A

Inverse correlation

209
Q

“Prostaglandin D synthase”

A

B-trace protein

210
Q

Established as an accurate marker of CSF leakage

A

B-trace protein

211
Q

Potential marker in detecting impaired renal function

A

B-trace protein

212
Q

Are proteolytic fragments of collagen I formed during bone resorption

A

Cross-linked C-telopeptides

213
Q

The process wherein osteoclasts breakdown the bone tissue

A

Resorption

214
Q

Biochemical marker of bone resorption

A

Cross-linked C-telopeptides

215
Q

Cross-linked C-telopeptides are detected in

A

Serum and urine

216
Q

A cysteine proteinase inhibitor

A

Cystatin C

217
Q

New sensitive endogenous serum marker for the glomerular filtration rate

A

Cystatin C

217
Q

Variety of conditions in which amyloid proteins are abnormally deposited in organs and/or tissues

A

Amyloidosis

217
Q

Insoluble fibrous protein aggregates formed due to an alteration in their secondary structure, in particular the β-pleated sheet form

A

Amyloids

218
Q

Help differentiate a diagnosis of Alzheimer disease from other forms of dementia

A

Amyloid β42 (Aβ42) and Tau protein tests

219
Q

Indication of Low Aβ42 and high Tau

A

Reflects increased likelihood of Alzheimer disease

220
Q

Transferrin-free protein that differentiates a CSF sample

A

Tau protein

221
Q

Rough measure of all of the proteins in the plasma

A

Total protein

222
Q

Decrease in blood protein concentration

A

Hypoproteinemia

223
Q

Causes of hypoproteinemia

A

Excessive loss
Malnutrition
Malabsorption
Liver diseases

224
Q

Increase in blood protein concentration

A

Hyperproteinemia

225
Q

Causes of hyperproteinemia

A

Dehydration
Excessive production of globulins (γ-globulins)

226
Q

Most abundant protein in plasma

A

Albumin

227
Q

Albumin is a negative acute-phase reactant protein. True or False?

A

True

228
Q

How to determine globulin fraction of albumin?

A

By subtracting the albumin from the total protein

229
Q

Indication when there is a characteristic beta-gamma (β-y) bridging

A

Cirrhosis

230
Q

Indication of increase in gamma (y)-globulins

A

Hepatitis

231
Q

Indication of increased alpha-2-globulin and beta-globulin fractions

A

Obstructive jaundice

232
Q

Measures all chemically bound nitrogen in the sample (either plasma or urine)

A

Total nitrogen

233
Q

Emission of light created from a chemical or electrochemical reaction

A

Chemiluminescence

234
Q

Principle of total nitrogen

A

Chemiluminescence

235
Q

Most commonly used sample for total protein

A

Serum

236
Q

Interferences of total protein

A

Lipemia
Hemolysis

237
Q

Reference range for serum total protein in adults

A

6.5 to 8.3 g/dL (65 to 83 g/L)

238
Q

Principle of Kjeldahl Method

A

Digestion of protein; measurement of nitrogen content

239
Q

Reference method in the quantitation of total protein

A

Kjeldahl Method

240
Q

Principle of Biuret Method

A

Formation of violet-colored chelate between Cu2+ ions and peptide bonds

241
Q

In biuret method, that absorbance of chelate is measure at

A

540 nm

242
Q

Routine method for total protein

A

Biuret Method

243
Q

Principle of Dye binding

A

Protein binds to dye and causes a spectral shift in the absorbance maximum of the dye

244
Q

Total Protein method used for research purposes

A

Dye binding

245
Q

Dyes used in dye-binding method

A

Ponceau S
Bromophenol blue
Methyl orange
HABA [2,4’-hydroxyazobenzene-benzoic acid]
Bromocresol green
Bromocresol purple
Amido black 10B
Lissamine green
Coomassie Brilliant Blue)

246
Q

Globulins are precipitated in high salt concentrations; albumin in supernatant is quantitated by biuret reaction

A

Salt precipitation

247
Q

Proteins separated based on electric charge

A

Electrophoresis

248
Q

Globulin is separated from albumin using sodium salts causing precipitation of globulin

A

Salt precipitation

249
Q

Most widely used methods for albumin determination

A

Dye binding

250
Q

Non-specific for albumin

A

Methyl orange

251
Q

Used to quantitate albumin

A

Bromocresol green
Bromocresol purple

252
Q

Support media used in albumin methods

A

Cellulose acetate
Agarose gel

253
Q

In electrophoresis, cation (+) migrates to

A

Cathode (-)

254
Q

In electrophoresis, anion (+) migrates to

A

Anode (+)

255
Q

List the serum proteins

A

Albumin
α1- globulins
α2-globulins
β-globulins
γ-globulins

256
Q

Serum protein that travels farthest to the anode

A

Albumin

257
Q

Reference values for serum protein electrophoresis

A

Albumin, 53% to 65% of the total protein (3.5 to 5.0 g/dL)
α1-Globulin, 2.5% to 5% (0.1 to 0.3 g/dL)
α2-Globulin, 7% to 13% (0.6 to 1.0 g/dL)
β-Globulin, 8% to 14% (0.7 to 1.1 g/dL)
γ-Globulin, 12% to 22% (0.8 to 1.6 g/dL)

258
Q

Decrease in the alpha 1 globulin

A

ALPHA 1 – ANTITRYPSIN DEFICIENCY

259
Q

Increase in alpha 2 globulin because of the presence of alpha 2 macroglobulin and haptoglobin
Decrease in albumin

A

NEPHROTIC SYNDROME

260
Q

Decrease in albumin.
Increase in alpha 1, alpha 2 and beta globulin

A

INFLAMMATION

261
Q

Beta-gamma bridging is a unique characteristic that is seen in patients with

A

CIRRHOSIS

262
Q

increase in immunoglobulin, result of monoclonal increase

A

MONOCLONAL INCREASE

263
Q

A condition in which abnormal proteins are found in the blood

A

Monoclonal gammopathy

264
Q

Separation of molecules in silica capillaries

A

CAPILLARY ELECTROPHORESIS

265
Q

Zone electrophoresis that separates proteins on the basis of pI (Isoelectric Point)

A

ISOELECTRIC FOCUSING

266
Q

Immunochemical Methods

A

Immunoturbidometry
Immunonephelometry

267
Q

Presence of proteinuria is often associated with renal disease. True or False?

A

True

268
Q

Principle of reagent strip test for protein

A

Protein error of indicator

269
Q

Reagent used in reagent strip test for protein

A

Tetrabromophenol blue or tetrachlorophenol tetrabromosulphonphthalein

270
Q

Quantitative test for urine protein

A

12 or 24-hour urine test

271
Q

Precipitation tests for protein

A

Trichloroacetic acid (TCA)
Salicylic Acid (SSA)
Benzethonium Chloride

272
Q

Presence of elevated levels of CSF protein is associated with damage to the blood-brain barrier. True or False?

A

True

273
Q

Common causes of damaged BBB

A

Meningitis
Hemorrhage

274
Q

Protein fraction used to evaluate the integrity of the blood brain barrier

A

CSF/Serum Albumin Index

275
Q

Protein fraction used to measure immunoglobulin G synthesis within the CSF

A

CSF IgG Index

276
Q

Elevated IgG in CSF is associated with

A

Multiple sclerosis

277
Q

Method to detect oligoclonal bands which indicate inflammation within the CSF

A

Electrophoresis

CLINICAL CHEMISTRY (10 decks)

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