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Clinical Chemistry 1 > C - Chapter VII: Proteins > Flashcards

C - Chapter VII: Proteins Flashcards

1
Q

PROTEINS
-covalently linked polymers of (?)

A

amino acids

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2
Q

PROTEINS
- amino acids are linked via (?) (formed upon removal of a water molecule)

A

peptide bond

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3
Q

PROTEINS
- synthesized in the liver & secreted by the hepatocyte into the circulation EXCEPT (?)

A

immunoglobulins (plasma cells)

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4
Q

PROTEIN
- provide (?) of the total daily body energy requirement

A

12 – 20%

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5
Q

PROTEINS
- composes (?) of the cell’s dry weight

A

50 – 70%

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6
Q
  • amphoteric
A

PROTEINS

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7
Q

sequence of the amino acids in the polypeptide chain

A

Primary structure

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8
Q

analytical processes:

A

chromatography, electrophoresis, dye binding and light absorbance depend on this sequence

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9
Q

arises from the interaction among the different segments of a polypeptide chain

A

Secondary structure

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10
Q

– chain forms a regular helix ; coil resembling a spring

A

a. alpha-helix

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11
Q

– in fully extended structures; flat, corrugated structure

A

b. beta-pleated sheets

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12
Q

– no apparent pattern

A

c. random coils

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13
Q

– actual 3-dimensional structure or folding pattern of the protein

A
  1. Tertiary structure
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14
Q

– association of several polypeptide chains into larger “oligomeric” aggregate unit

A
  1. Quaternary structure
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15
Q

stable complexes:

A

dimers, trimers, tetramers

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16
Q

Classification

A
  1. Simple
  2. Conjugated
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17
Q

contain peptide chains that on hydrolysis yield only AA

A
  1. Simple
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18
Q

protein (apoprotein) + nonprotein (prosthetic group)

A
  1. Conjugated
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19
Q

prosthetic group :

A

lipid (lipoprotein) , carbohydrate (glycoprotein) , metals (metalloprotein) , etc.

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20
Q

: relatively symmetrical with compactly folded and coiled polypeptide chains

A

a. globular

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21
Q

: more elongated and asymmetrical and have a higher viscosity

A

b. fibrous

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22
Q

Functions
- Repair (?)
- Important in (?)
- For transport of (?)
- Maintenance of (?)
- Maintenance of (?) (buffers)
- Bio-(?)

A

body tissues
blood coagulation and immunologic function
metabolic substances
osmotic pressure
blood pH
-catalysts

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23
Q

Metabolism

A
  1. Dietary Intake
  2. Absorption
  3. Production
  4. Storage
  5. Destruction
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24
Q

MAJOR PLASMA PROTEINS

A
  1. PRE-ALBUMIN (Transthyretin)
  2. ALBUMIN
  3. GLOBULINS
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25
Q

− Migrates ahead of albumin

A
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26
Q

− Rich in tryptophan and contain 0.5% carbohydrate

A

PRE-ALBUMIN (Transthyretin)

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27
Q

− Serves as transport protein for T3, T4 and retinol (Vit. A)

A

PRE-ALBUMIN (Transthyretin)

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28
Q

− Increased: alcoholism, chronic renal failure, steroid treatment

A

PRE-ALBUMIN (Transthyretin)

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29
Q

− Decreased: poor nutrition, liver disorder, malignancy

A

PRE-ALBUMIN (Transthyretin)

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30
Q

− largest plasma protein fraction (52-62%)

A

ALBUMIN

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31
Q

− synthesized in the liver at a rate that is dependent on protein intake

A

ALBUMIN

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32
Q

− serves as circulating reservoir of amino acids

A

ALBUMIN

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33
Q

− regulator of osmotic pressure

A

ALBUMIN

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34
Q

− transport protein because of ease of binding with blood components

A

ALBUMIN

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35
Q

− a “negative acute phase reactant”

A

ALBUMIN

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36
Q

− sensitive & highly prognostic marker in cases of cystic fibrosis

A

ALBUMIN

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37
Q

ALBUMIN

Reference values:

A

3.5 – 5.0 g/dL (35 – 50 g/L)

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38
Q

Increased − hemoconcentration, dehydration

A

ALBUMIN

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39
Q

Increased
− excessive infusion

A

albumin (Hyperalbuminemia)

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40
Q

− decreased synthesis (liver impairment)

A

Decreased albumin (Hypoalbuminemia)

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41
Q

− malabsorption or malnutrition

A

Decreased albumin (Hypoalbuminemia)

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42
Q

Decreased − nephrotic syndrome (renal loss)

A

albumin (Hypoalbuminemia)

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43
Q

Decreased − severe burns

A

albumin (Hypoalbuminemia)

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44
Q

– heterogenous complex mixture of protein molecules (α1, α2, β and γ fractions)

A

GLOBULINS

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45
Q

Elevated concentration of globulin in early cirrhosis will balance loss of albumin resulting to normal levels of total protein

A

GLOBULINS

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46
Q

GLOBULINS

normal A/G ratio :

A

1.3 – 3 : 1

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47
Q

GLOBULINS

low A/G ratio

A

– liver diseases, infectious diseases, multiple myeloma, nephritis

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48
Q

Alpha1-globulins

A

a. α-1-antitrypsin
b. α-1-fetoprotein
c. α-1-Acid Glycoprotein (orosomucoid)
d. α-1-Antichromotrypsin

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49
Q

Alpha2-globulins

A

A. Haptoglobin
B. Ceruloplasmin

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50
Q

Beta-globulins

A

a. Transferrin (Siderophilin)
b. β2-Microglobulin

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51
Q

GLOBULINS

A

(1) Alpha1-globulins
(2) Alpha2-globulins
(3) Beta-globulins
(4) GAMMA-GLOBULINS
(5) FIBRINOGEN
(6) LIPOPROTEIN
(7) COMPLEMENT
(8) C-REACTIVE PROTEIN

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52
Q

– 90% of the α1-globulin band

A

α-1-antitrypsin

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53
Q
  • an acute phase reactant
A

α-1-antitrypsin

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54
Q
  • neutralize trypsin-like enzymes
A

α-1-antitrypsin

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55
Q
  • major inhibitor of protease activity
A

α-1-antitrypsin

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56
Q

inhibit lysosomal elastase released from PMNs during their

A

α-1-antitrypsin

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57
Q
  • Increased: inflammation, pregnancy and contraceptive use
A

α-1-antitrypsin

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58
Q
  • Decrease: associated with emphysematous pulmonary disease & juvenile hepatic cirrhosis
    a. α-1-antitrypsin
    b. α-1-fetoprotein
    c. α-1-Acid Glycoprotein
A

α-1-antitrypsin

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59
Q

synthesized initially by the fetal yolk sac & then the parenchymal cells of the liver

A
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60
Q
  • used as a tumor marker (hepatic & gonadal CA)
A

a-1-fetoprotein

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61
Q
  • screening test for any fetal conditions, increase passage of fetal proteins into the amniotic fluid; detects neural tube defects
A

a-1-fetoprotein

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62
Q
  • Increased: neural tube defects (spina bifida), atresia of the GIT, fetal distress, ataxia telangiectasia, tyrosinosis, hemolytic disease of the newborn (HDN)
A

α-1-fetoprotein

63
Q
  • Decreased: Down’s syndrome
A

α-1-fetoprotein

64
Q
  • contains high percentage of CHO and sialic acid (45% CHO + 11-12% Sialic acid)
A

α-1-Acid Glycoprotein (orosomucoid)

65
Q
  • synthesized both by the liver & by granulocytes and monocytes
A

α-1-Acid Glycoprotein (orosomucoid)

66
Q
  • inhibits the phagocytic activity of neutrophils & inhibits platelet aggregation
A

α-1-Acid Glycoprotein (orosomucoid)

67
Q
  • may inactivate progesterone
A

α-1-Acid Glycoprotein (orosomucoid)

68
Q

Increased: pregnancy, cancer, pneumonia, rheumatoid arthritis (RA), cell proliferation

A

α-1-Acid Glycoprotein (orosomucoid)

69
Q

Decreased: nephrotic syndrome

A

α-1-Acid Glycoprotein (orosomucoid)

70
Q

Alpha1-globulins

A

a. α-1-antitrypsin
b. α-1-fetoprotein
c. α-1-Acid Glycoprotein (orosomucoid)
d. α-1-Antichromotrypsin

71
Q

an acute phase reactant

A

α-1-antitrypsin
Haptoglobin
FIBRINOGEN

72
Q
  • synthesized in the hepatocytes & cells of the RES
A

Haptoglobin

73
Q
  • binds free hemoglobin by its α- chain
A

Haptoglobin

74
Q
  • one of the proteins used to evaluate rheumatic diseases
A

Haptoglobin

75
Q

Increased: inflammation, nephrotic syndrome, burns, trauma

A

Haptoglobin

76
Q

Decreased: intravascular hemolysis and liver disease

A

Haptoglobin

77
Q

copper-containing protein BUT does NOT transport copper

A

Ceruloplasmin

78
Q

synthesized in the liver, where 6-8 copper atoms are attached

A

Ceruloplasmin

79
Q
  • serves as an antioxidant to prevent lipid peroxidation & cellular damage
A

Ceruloplasmin

80
Q
  • increased in inflammation and pregnancy
A

Ceruloplasmin

81
Q
  • indicator for Wilson’s disease (0.1 g/L)
A

Ceruloplasmin

82
Q

Ceruloplasmin

  • Decreased: Wilson’s disease, malnutrition, malabsorption, nephrotic disease, Menke’s disease (kinky hair syndrome)
A

Wilson’s disease, malnutrition, malabsorption, nephrotic disease, Menke’s disease (kinky hair syndrome)

83
Q

– largest major non-immunoglobulin protein in plasma

A

α-2-Macroglobulin

84
Q
  • found principally in the intravascular spaces; does not diffuse from the plasma space
A

α-2-Macroglobulin

85
Q
  • lower amounts can also be found in CSF
A

α-2-Macroglobulin

86
Q
  • inhibits proteases such as trypsin, pepsin and plasmin
A

α-2-Macroglobulin

87
Q
  • major component of the β2-globulin fraction
A

Transferrin (Siderophilin)

88
Q
  • a glycoprotein synthesized in the liver
A

Transferrin (Siderophilin)

89
Q
  • transports oxidized iron (Fe+3)to its storage sites
  • prevents loss of iron through the kidney
A

Transferrin (Siderophilin)

90
Q

Increased: hemochromatosis (bronze skin)

A

Transferrin (Siderophilin)

91
Q

Decreased: liver disease, malnutrition, nephrotic syndrome

A

Transferrin (Siderophilin)

92
Q
  • light chain component of the major human leukocyte antigen (HLA)
A

β2-Microglobulin

93
Q
  • found on the surface of most nucleated cells
A

β2-Microglobulin

94
Q
  • present in high concentration on lymphocytes
A

β2-Microglobulin

95
Q
  • filtered by the renal glomerulus but reabsorbed
A

β2-Microglobulin

96
Q

Increased: RA, systemic lupus erythematosus (SLE), HIV

A

β2-Microglobulin

97
Q

Increased in:
• chronic inflammation
• cirrhosis or viral hepatitis
• collagen diseases
• paraproteins (monoclonal bands, gammopathies)

A

GAMMA-GLOBULINS

98
Q

Decreased in: congenital or acquired immunodeficiency
(4) GAMMA-GLOBULINS
(5) FIBRINOGEN
(7) COMPLEMENT

A

GAMMA-GLOBULINS

99
Q

– synthesized in the plasma cells

A

Immunoglobulins

100
Q
  • not produced to any extent by the neonate
A

Immunoglobulins

101
Q

– one of the largest proteins in the blood plasma

A

FIBRINOGEN

102
Q
  • synthesized in the liver
A

FIBRINOGEN

103
Q
  • most abundant of the coagulation factors
A

FIBRINOGEN

104
Q
  • an acute phase reactant; markedly increased during inflammatory process
A

FIBRINOGEN

105
Q
  • may serve as a marker for long-term prognosis of cardiovascular disease
A

FIBRINOGEN

106
Q
  • distinct band between β and γ-globulins on electrophoresis
A

FIBRINOGEN

107
Q
  • it forms a fibrin clot when activated by thrombin
A

FIBRINOGEN

108
Q

Increased: pregnancy and use of birth control pills

A

FIBRINOGEN

109
Q

FIBRINOGEN Decreased:

Reference values:

A

extensive coagulation

200 – 400 mg/dL (2.0 -4.0 g/L)

110
Q
  • complexes of proteins & lipids (LDL, HDL, VLDL, Chylomicrons)
A

LIPOPROTEIN

111
Q
  • transports cholesterol, triglyceride and phospholipids
A

LIPOPROTEIN

112
Q
  • participates in the immune reaction and serve as a link to the inflammatory response
A

COMPLEMENT

113
Q
  • circulates as non-functional precursors
A

COMPLEMENT

114
Q

Increased: inflammatory states

A

COMPLEMENT

115
Q

Decreased: SLE, DIC, malnutrition

A

COMPLEMENT

116
Q
  • appears in blood of patients with diverse inflammatory diseases
A

C-REACTIVE PROTEIN

117
Q
  • undetectable in healthy individuals
A

C-REACTIVE PROTEIN

118
Q
  • precipitates with the C substance, a polysaccharide of pneumococci
A

C-REACTIVE PROTEIN

119
Q
  • general scavenger molecule; gamma-migrating protein
A

C-REACTIVE PROTEIN

120
Q

Increased: acute rheumatic fever, MI, RA, gout, bacterial & viral infections

A

C-REACTIVE PROTEIN

121
Q

MISCELLANEOUS PROTEINS:

A
  1. Myoglobin
  2. Troponins
  3. Amyloid
122
Q

▪ A heme protein or oxygen-binding transport protein found in skeletal and cardiac muscles

A

Myoglobin

123
Q

▪ Approximately 2% of the total muscle protein

A

Myoglobin

124
Q

▪ Marker for chest pain (angina) and early detection of acute myocardial infarction (AMI)

A

Myoglobin

125
Q

▪ In AMI, the onset is [?], peak level [?], normalize in [?]

A

1-3 hours
5-12 hours
18-30 hours

126
Q

▪ Useful marker for monitoring the success or failure of reperfusion

A

Myoglobin

127
Q

Increased: AMI, angina, rhabdomyolysis, muscle trauma, extrenuous exercise, IM injection

A

Myoglobin

128
Q

▪ A complex of 3 proteins that bind to the thin filaments of striated muscle (cardiac & skeletal)

A

Troponins

129
Q

▪ Diagnostic marker for identifying cardiac injury in the presence of a skeletal muscle damage

A

Troponins

130
Q

▪ Levels in blood may elevate after AMI in the absence of CK-MB elevations

A

Troponins

131
Q

▪ TnT, TnI, TnC = muscle contraction

A

Troponins

132
Q

▪ A pathological extracellular deposit associated with a group of disorders collectively called amyloidosis.

A

Amyloid

133
Q

Ultimate product of digestion

A

Amino acids

134
Q

Enumerate hormones which promote protein synthesis

A

Growth hormone
Insulin
Thyroid hormone

135
Q

A type of protein which is formed when the segments of the polypeptide chain interact with one another

A

Secondary structure

136
Q

The secondary structure is maintained by this type of bond

A

Hydrogen bond

137
Q

A heme containing protein which binds oxygen and skeletal muscles

A

Myoglobin

138
Q

Which of the following proteins contains copper and functions as a peroxidase enzyme

A

Ceruloplasmin

139
Q

Based on electrophoretic mobility, ceruloplasmin belongs to this type of fraction

A

Alpha-2-globulin

140
Q

Among the different classes of proteins, which is a negative acute phase reactant

A

Albumin

141
Q

An assay performed on this protein serves as presumptive or differential diagnosis of bacterial and viral infection

A

C-reactive Protein

142
Q

This protein is a light chain component the major Human Leukocyte Antigen

A

Beta-2-microglogulin

143
Q

Which of the following white blood cells contain a high concentration of beta-2-microglogulin

A

Lymphocytes

144
Q

This protein forms a distinct bond between beta and gamma globulins on plasma electrophoresis

A

Fibrinogen

145
Q

A decrease of this protein on maternal serum during pregnancy is associated with down’s syndrome

A

Alpha-1-fetoprotein

146
Q

Also known as pre-albumin

A

Transthyretin

147
Q

Pre-albumin is rich in the amino acid

A

Tryptophan

148
Q

The protein that binds with free hemoglobin is

A

Haptoglobin

149
Q

Based on electrophoretic mobility, haptoglobin belongs to this type of fraction

A

Alpha-2-globulin

150
Q

The deposition of this protein is common among patients with cystic fibrosis

A

Albumin

151
Q

In the presence of hemolytic disorders, the plasma level of haptoglobin…

A

Decreases

152
Q

Identify the proteins which form complexes with trypsin in the circulation and cause its inactivation

A

Alpha-1-antitrypsin
Alpha-2-macroglobulin

153
Q

The largest major non immunoglobulin protein in plasma is

A

Alpha-2- macroglobulin

154
Q

An assay of this protein is currently considered the gold standard and laboratory diagnosis of acute myocardial infarction

A

Troponin

Clinical Chemistry 1 (10 decks)

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