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Clinical Chemistry 1 (Semis) > LAB: Amino Acids & Proteins > Flashcards

LAB: Amino Acids & Proteins Flashcards

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1
Q

It regulates the distribution of amino acids.

A

Liver

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2
Q

In the stomach, this breaks down proteins into peptides.

A

Pepsin

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3
Q

Amino acid absorption occurs from the ________ into the blood stream

A

small intestine

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4
Q

In what organ does the enzymes break peptides into amino acids?

A

Small intestine

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5
Q

Enumerate the enzymes secreted by the stomach cells

A
  • Pepsin
  • Hydrochloric acid (HCl)
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5
Q

Enumerate the enzymes secreted by the acinar cells of pancreas

A
  • Trypsin
  • Chymotrypsin
  • Elastase
  • Sodium bicarbonate
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5
Q

Enumerate the enzymes secreted by the intestinal cells

A
  • Secretin
  • Cholecystokinin (CCK)
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5
Q

Based on chemical properties, what are the amino acids that are aromatic

A
  • Phenylalanine
  • Tyrosine
  • Tryptophan
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6
Q

Based on chemical properties, what are the amino acids that are negatively charged

A
  • Aspartic acid
  • Glutamatic acid
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6
Q

Based on nutritional requirements, what are the essential amino acids

A
  • Isoleucine
  • Leucine
  • Lysine
  • Methionine
  • Phenylalanine
  • Threonine
  • Tryptophan
  • Valine
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6
Q

Based on nutritional requirements, what are the semi- essential amino acids

A
  • Arginine
  • Histidine
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6
Q

Based on chemical properties, what are the amino acids that are positively charged

A
  • Lysine
  • Arginine
  • Histidine
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7
Q

Based on nutritional requirements, what are the non-essential amino acids

A
  • Alanine
  • Asparagine
  • Aspartic acid
  • Cysteine
  • Glutamic acid
  • Glutamine
  • Glycine
  • Hydroxylysine
  • Hydroxyproline
  • Proline
  • Serine
  • Tyrosine
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8
Q

What are the stop codons

A
  • UAA
  • UAG
  • UGA
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9
Q

What is the start codon

A

AUG

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10
Q

Refers to the number, type, and sequence of amino acids in the polypeptide chain

A

Primary structure

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11
Q

Refers to commonly formed arrangements stabilized by hydrogen bonds between nearby amino acids within the protein

A

Secondary structure

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12
Q

Refers to the overall shape,
or conformation, of the protein molecule

A

Tertiary structure

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13
Q

The shape or structure that results from the interaction of more than one protein molecule, or protein subunits, referred to as a multimer, that functions as a single unit.

A

Quaternary structure

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14
Q

Are a class of inborn errors of metabolism in which an enzyme defect inhibits the body’s ability to metabolize certain amino acids

A

Aminoacidopathies

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15
Q

May also be analyzed to aid in the diagnosis of select neurotransmitter disorder

A

Cerebrospinal fluid (CSF)

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16
Q

Blood samples for amino acid analysis should be drawn after how many hours of fasting?

A

6 to 8 hours

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17
Q

For amino acid analysis, the sample should be collected in a _________ tube and the plasma removed from the cells within _______ of collection.

A

heparinized and 2 hours, respectively

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18
Q

For quantitation of urinary amino acid what sample is preferred?

A

a well-mixed aliquot from a first morning collection

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19
Q

If testing is to be delayed, samples can be refrigerated up to _______or frozen for up to ______.

A

24 hours and 1 month, respectively

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20
Q

This may be used to quantitate amino acids and their metabolites in the patient sample

A

high-performance liquid chromatography coupled with tandem mass spectrometry (HPLC-MS/MS)

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21
Q

Considered to have higher specificity and greater sensitivity allowing for detection of lower concentrations of the amino acid(s) and an earlier diagnosis

A

MS/MS methods

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22
Q

Performed to aid in the diagnosis and detection of carrier status in families with an inborn error of metabolism

A

Genetic assays using DNA analysis or DNA analysis

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23
Q

The pH at which an amino acid or protein has no net charge is known as

A

isoelectric point (pI)

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24
Q

When the pH is greater than the pI, the protein has a _________________, and when the pH is less than the pI, the protein has a _________________.

A

net negative charge and net positive charge, respectively

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25
Q

Proteins differ in their pI values, but most occur in the pH range of

A

5.5 to 8.0

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26
Q

Suppresses proteolysis

A

Insulin

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27
Q

Stimulates protein synthesis

A

Growth Hormone

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28
Q

Stimulates protein degradation in muscles

A

Glucocorticoids

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29
Q

Increases protein deposition in tissues

A

Sex Hormones

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30
Q

Inhibits proteolysis in fasting state, but stimulates protein synthesis in fed state

A

Insulin-like Growth Factor-1

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31
Q

Promotes uptake of amino acids in the liver

A

Glucagon

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32
Q

Increases protein deposition in tissues

A

Sex Hormones

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33
Q

Increases production of gluconeogenic amino acids

A

Catecholamines

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34
Q

Increases the basal metabolic rate

A

Thyroxine

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35
Q

Are proteins that catalyze biochemical reactions. They are normally found intracellularly and are released into the bloodstream when tissue damage occurs, making enzyme measurements an important diagnostic tool

A

Enzymes

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36
Q

Are chemical messenger proteins that control the action(s) of specific cells or organs. They directly affect growth and development, metabolism, sexual function, reproduction, and behavior

A

Hormones

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37
Q

Are proteins that are produced by B cells (lymphocytes) in the bone marrow. They mediate the humoral immune response to identify and neutralize foreign antigens

A

Immunoglobulins or antibodies

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38
Q

Are fibrous proteins that provide structure to many cells and tissues throughout the body, such as muscle, tendons, and bone matrix

A

Structural proteins

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39
Q

Serve as reservoirs for metal ions and amino acids so they can be stored without causing harm to the cell and released when needed

A

Storage proteins

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40
Q

Routine analysis of blood specimens will typically include measurement of

A
  • Measurement of total protein and albumin
  • Albumin-to-globulin (A/G) ratio
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41
Q

The relationship between pH, pKa, and charge for individual amino acids can be described by the

A

Henderson-Hasselbalch equation

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42
Q

Cite the Henderson-Hasselbalch equation

A

pH = pKa + log [conjugate base]/ [conjugate acid]

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42
Q

Indicator of nutrition; binds thyroid hormones and retinol- binding protein

A

Prealbumin or transthyretin

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43
Q

Binds bilirubin, steroids, fatty acids; major contributor to oncotic pressure

A

Albumin

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44
Q

FUNCTION OF PROTEINS: Maintenance of water distribution between cells and tissue, interstitial compartments, and the vascular system of the body

A

Osmotic force

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45
Q

FUNCTION OF PROTEINS: Participation as buffers to maintain pH

A

Acid-base balance

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46
Q

FUNCTION OF PROTEINS: participation in coagulation of blood

A

Hemostasis

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47
Q

FUNCTION OF PROTEINS: Tissue nutrition

A

Energy

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48
Q

FUNCTION OF PROTEINS: Metabolic substances

A

Transport

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49
Q

FUNCTION OF PROTEINS:
Connective tissue

A

Structure

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50
Q

Acute-phase reactant; protease inhibitor

A

α1-Antitrypsin

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51
Q

Principal fetal protein; elevated levels indicate risk for spina bifida

A

α1-Fetoprotein

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52
Q

Acute-phase reactant; transport of drugs and hormones

A

α1-Acid glycoprotein (orosomucoid)

53
Q

Lipid transport (HDL)

A

α1-Lipoprotein

53
Q

Transports vitamin D and binds actin

A

Gc-globulin

54
Q

Acute-phase reactant, oxidase activity; contains copper

A

Ceruloplasmin

55
Q

Transports lipids (primarily VLDL triglyceride)

A

Pre-β lipoprotein

56
Q

Component of human leukocyte antigens (HLA)

A

β2-Microglobulin (B2M)

57
Q

Acute-phase reactant; may be related to immune responses

A

α1-Acid glycoprotein (orosomucoid)

58
Q

Transports iron

A

Transferrin

59
Q

Binds heme

A

Hemopexin

60
Q

Transports lipids (primarily LDL cholesterol)

A

β-Lipoprotein

61
Q

Precursor to fibrin

A

Fibrinogen

62
Q

Acute-phase reactant; motivates phagocytosis in inflammatory disease

A

C-Reactive Protein (CRP)

63
Q

Antibodies (in secretions)

A

Immunoglobulin A

64
Q

Antibodies (early response)

A

Immunoglobulin M

65
Q

Antibodies (reagins, allergy); promotes release of histamine (allergies)

A

Immunoglobulin E

66
Q

Reference range for Total Protein - Serum, Plasma:

A

Adult: 6.5-8.3 g/dL (65-83 g/L)

67
Q

Reference range for Albumin- Serum, Plasma:

A

Adult: 3.5-5.5 g/dL (35-55 g/L)

68
Q

Reference range for Albumin-Globulin Ratio (A/G) - Serum, Plasma:

A

Adult: 1.1-1.8

69
Q

Enumerate the other proteins

A
  • Troponins
  • Natriuretic peptides
  • Myoglobins
  • Fibronectins
  • Cystatin-C
70
Q

They are considered the gold standard for diagnosis of acute coronary syndrome (ACS), in which the blood supply to the heart muscle is suddenly impeded

A

Cardiac troponin (cTn) which consists of troponin C (TnC), troponin I (cTnI), and troponin T (cTnT)

71
Q

Neurohormones that affect body fluid homeostasis, through natriuresis and diuresis, and blood pressure, through decreased angiotensin II and norepinephrine synthesis

A

Natriuretic Peptides

72
Q

Used to help predict the short-term risk of premature delivery

A

Fetal fibronectin (fFN)

73
Q

A proteolytic fragment of type I collagen crosslinked at the N- and C-terminal ends of the molecule and formed during bone resorption

A

Cross-linked C-telopeptide (CTX)

74
Q

A low-molecular-weight protease inhibitor produced by all nucleated cell. Used to evaluate glomerular function in individuals for whom creatinine measurements may be misleading, such as patients with cirrhosis, obesity, malnutrition, or who have a reduced muscle mass

A

Cystatin C

75
Q

Refers to conditions in which the serum or plasma total protein concentration is below the reference range

A

Hypoproteinemia

76
Q

An increase in total plasma proteins, is not generally associated with a specific disease state, but rather, it is more likely the result of dehydration

A

Hyperproteinemia

77
Q

Cite atleast two applications of molecular size

A
  • Gel chromatography
  • Ultracentrifugation
  • Gradient pore electrophoresis
  • Mass spectrometry
78
Q

Cite atleast two applications of solubility

A
  • Protein precipitation
  • Turbidimetry
  • Nephelometry
79
Q

Cite atleast two applications of Charge

A
  • Serum protein electrophoresis
  • Isoelectric focusing
  • Immunofixation electrophoresis
  • Ion exchange chromatography
80
Q

Cite atleast two applications of Molecular Interactions

A
  • Affinity chromatography
  • Immunoassays
  • Immunoelectrophoresis
  • Immunofixation
  • Dye-binding
81
Q

For testing other proteins, plasma samples should be collected using a?

A

plasma separator tube

82
Q

For protein analysis, cite the physical methods under the quantitative type

A
  • Dye binding
  • Direct Absorbance Measurements
  • Protein Ligands
  • Precipitation
  • Mass Spectrometry
82
Q

Collected in a serum separator tube and are preferred for protein analyses due to the presence of fibrinogen in plasma

A

Serum

82
Q

For protein analysis, cite the activity measurements under the quantitative type

A
  • Binding protein
  • Protease inhibitors
  • Complement factors
  • Coagulation factors
82
Q

Enumerate the quantitative methods for protein analysis

A
  • Physical methods
  • Activity measurements
  • Immunoassays
82
Q

Acid digestion is used to convert protein nitrogen into ammonium ions, which are then quantified

A

Kjeldahl Method

83
Q

Enumerate the qualitative methods for protein analysis

A
  • Electrophoresis
  • Chromatography
  • Genetic Analysis
  • Functional Assays
  • Mass Spectrometry
84
Q

Principle: Dye binds to protein causing a spectral shift in the absorbance maximum of the dye

A

Dye binding

84
Q

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

A

Biuret Method

85
Q

Principle: Proteins in solution absorb UV light with maximum absorbances of 200 and 280 nm

A

Ultraviolet (UV)
absorption

86
Q

Principle: Formation of aggregates by protein precipitation or antibody-binding that affect light scatter

A

Turbidimetry & Nephelometry

87
Q

Principle: Migration of proteins based on their density and charge under the influence of an electric field

A

Protein electrophoresis

88
Q

Used in automated protein measurements and to quantitate proteins separated by electrophoresis

A

Dye binding

89
Q

Routine method; requires at least two peptide bonds and an alkaline medium

A

Biuret method

90
Q

Immunoturbidimetric and immunonephelometric methods used to quantitate specific proteins

A

Turbidimetry & Nephelometry

91
Q

Limited utility for protein mixtures due to variable absorption characteristics; potential use in measurement of specific fractions after separation by another method

A

Ultraviolet (UV) absorption

92
Q

Used to separate and quantify protein fractions in serum, urine, and cerebrospinal fluid

A

Protein electrophoresis

93
Q

In Kjeldahl method, to correct for the average nitrogen content of protein, you multiply with?

A

6.25

94
Q

Transerythrin is stimulated by hormones:

A
  • Glucocorticosteroids
  • Androgens
  • NSAIDS (Aspirin)
95
Q

Synthesized in the liver and lesser extent from CSF (choroid plexus)

A

Prealbumin or Transerythrin

96
Q

Prealbumin Diagnosis:

A
  • Inflammation and Malignancy
  • Cirrhosis of the liver
  • Protein-losing diseases of the gut or kidneys
  • Familial euthyroid hyperthyroxinemia
97
Q

Reference interval for Prealbumin

A

20-40 mg/dL

98
Q

Laboratory tests used for prealbumin

A
  • Serum electrophoresis
  • Immunoturbidimetric or Immunonephelometric
99
Q

The major protein component of the most extravascular body fluids

A

Albumin

100
Q

Albumin is increased in:

A
  • Dehydration
  • Prolonged tourniquet application
101
Q

Albumin is decreased in:

A
  • Analbuminemia
  • Inflammation
  • Hepatic disease
  • Urinary loss
  • Gastrointestinal loss
  • Protein- energy malnutrition (Marasmus)
  • Burn injury
  • Edema and ascites
102
Q

Reference interval for Albumin

A

35-52 g/L or 3500-5200 mg/dL

102
Q

The most widely used methods for determining albumin are

A

bromocresol green (BCG) or bromocresol purple (BCP)

103
Q

Enumerate the disadvantages of Kjeldahl method

A
  • Time-consuming
  • Inconvenient
  • Impractical for routine use
104
Q

What dyes are used to stain protein after electrophoresis?

A
  • Bromophenol blue
  • Ponceau S
  • Amido black
  • Lissamine green
  • Coomassie brilliant blue
105
Q

Laboratory tests for Albumin

A
  • Dye binding
  • Serum electrophoresis
  • Immunoturbidimetry, immunoelectrophoresis, and immunofixation electrophoresis
  • Nephelometry
  • Isoelectric focusing
106
Q

This separates proteins on the basis of their electric charge and density across a support
media

A

Electrophoresis

107
Q

What are the support medias are used in electrophoresis

A

Agarose gel or cellulose acetate

108
Q

This show a dramatic decrease in the relative amounts of albumin, al -globulins, B-globulins, and y-globulins and an apparent increase in the a2 -globulin fraction

A

Nephrotic syndrome

108
Q

Decreased or absent a1- globulin fraction is associated with a1 -antitrypsin deficiency, as a1 -antitrypsin accounts for approximately 90% of the a1 -globulin fraction

A

Alpha-1 Antitrypsin deficiency

109
Q

Normal except for alpha2-globulin

A

Acute phase proteins

110
Q

Defective gamma globulins which results to defective or absent immunoglobulins; common to HIV patients

A

Hypogammaglobulinemia

111
Q

Increase results in all y-globulin

A

Polyclonal gammopathies

112
Q

Increase results in a single homogenous spike (M protein) in the y-globulin region

A

Monoclonal gammopathies

113
Q

Increases in fast-moving γ-globulins, such a IgA, prevent resolution of the β- and γ-globulin bands, resulting in a β–γ bridge

A

Liver cirrhosis

114
Q

Shows a relative decrease in albumin, α1 -globulins, α2- globulins, and β-globulins, with a relative increase in γ-globulin

A

Severe hepatic damage

115
Q

IDENTIFY THE DISEASE based on TPAG levels:
- Total Protein- normal, decrease
- Albumin- decrease
- Globulin- increase

A
  • Hepatic damage
    Cirrhosis B-Y bridging
    Hepatitis ↑ y- globulins
    Obstructive jaundice ↑ a2, B-globulins
  • Burns, trauma
  • Infection
    Acute ↑ a1-, a2- globulins
    Chronic ↑ a1, a2, y- globulins
116
Q

IDENTIFY THE DISEASE based on TPAG levels:
- Total Protein- decrease
- Albumin- decrease
- Globulin- normal

A
  • Malabsorption
  • Inadequate diet
  • Nephrotic syndrome ↑ a2-, B-globulins, ↓ y-globulins
116
Q

IDENTIFY THE DISEASE based on TPAG levels:
- Total Protein- decrease
- Albumin- normal
- Globulin- decrease

A

Immunodeficiency syndromes

117
Q

IDENTIFY THE DISEASE based on TPAG levels:
- Total Protein- decrease
- Albumin- decrease
- Globulin- decrease

A

Salt retention syndrome

118
Q

IDENTIFY THE DISEASE based on TPAG levels:
- Total Protein- increase
- Albumin- increase
- Globulin- increase

A

Dehydration

119
Q

IDENTIFY THE DISEASE based on TPAG levels:
- Total Protein- increase
- Albumin- normal
- Globulin- increase

A
  • Multiple myeloma
  • Monoclonal and polyclonal gammopathies
120
Q

Rapid, easy to use; unequal sensitivity for individual proteins

A

Turbidimetric methods
(sulfosalicylic acid, trichloroacetic acid, or benzethonium chloride)

121
Q

This urine protein method is accurate

A

Biuret

122
Q

This urine protein method is very sensitive

A

Folin-Lowry

123
Q

Initial biuret reaction; oxidation of tyrosine, tryptophan, and histidine residues by phenol reagent; measurement of resultant blue color

A

Folin-Lowry

124
Q

This urine protein method is used in automated methods

A

Dye binding (pyrogallol red)

125
Q

Reference Ranges for Urine Protein Analyses:

Total Protein—Urine, 24-hour

A

Adult: <150 mg/24 hours

126
Q

Reference Ranges for Urine Protein Analyses:

Protein/Creatinine Ratio- Urine, 24-Hour

A

Adult: ≤0.114 mg/mg creatinine

127
Q

Reference Ranges for CSF Protein Analyses:

Total Protein - CSF

A
  • 0–7 days: 40–120 mg/dL
  • 8 days–1 month: 20–40 mg/dL
  • > 1 month: 14–45 mg/dL
128
Q

Reference Ranges for CSF Protein Analyses:

Albumin- CSF

A

0-35 mg/dL

129
Q

Reference Ranges for CSF Protein Analyses:

CSF- Serum Albumin Ratio

A

2.7- 7.3

130
Q

Reference Ranges for CSF Protein Analyses:

IgG INDEX

A

0.26–0.70

131
Q

IgG index formula

A

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Clinical Chemistry 1 (Semis) (2 decks)

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