PROTEIN Flashcards

aralllll fles

1
Q

sequence of the AA in the polypeptide chain (linear)

A

Primary Structure

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2
Q

determines the overall shape of the protein

A

Primary Structure

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3
Q

Analytical processes of primary structure

A
  • chromatography
  • electrophoresis
  • dye binding
  • light absorbance
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4
Q

Analytical processes: chromatography, electrophoresis, dye binding and light absorbance depends on this sequence

A

Primary sequence

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5
Q

conformation of the segments of the polypeptide chain

A

Secondary structure

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6
Q

secondary structure maintained by:

A

Hydrogen Bond

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7
Q

Important for the strength and flexibility of proteins

A

secondary structure

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8
Q

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

A

secondary structure

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9
Q

3 structures of secondary structure

A
  • Alpha-Helix
  • Beta-Pleated sheets
  • Random coils
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10
Q

Chain forms a regular helix; coil
resembling a spring

A

Alpha-Helix

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11
Q

In fully extended structures; flat, corrugated structure

A

Beta-Pleated sheets

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12
Q

secondary structure that has no apparent pattern

A

Random coils

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13
Q

Actual 3-dimensional structure of folding pattern of the protein

A

Tertiary Structure

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14
Q

tertiary structure is maintained by

A

covalent disulfide bond

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15
Q

responsible for many of the physical and chemical properties of proteins

A

tertiary structure

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16
Q

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

A

quaternary structure

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17
Q

Quaternary structure is an association of several polypeptide chains into larger_

A

“oligomeric” aggregate unit

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18
Q

quaternary structure is maintained by_

A

non-covalent bond (hydrogen bond)

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19
Q

stable complexes of quaternary structure

A
  • dimers
  • trimers
  • tetramers
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20
Q

examples of quaternary structure

A
  • hemoglobin
  • lactate dehydrogenase
  • creatine phosphokinase
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21
Q

factors that cause loss of functions of proteins:

A
  • heat
  • hydrolysis by strong acid or alkali
  • enzymatic reaction
  • exposure to UV light
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22
Q

contain peptide chains that hydrolysis yield only AA

A

simple proteins

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23
Q

relatively symmetrical with compactly folded and coiled polypeptide chains

A

globular

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24
Q

examples of globular simple proteins

A
  • hemoglobin
  • plasma proteins
  • enzymes
  • peptide hormones
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25
Q

more elongated and asymmetrical and have a higher viscosity

A

fibrous

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26
Q

examples of fibrous simple protein

A
  • fibrinogen
  • troponin
  • collagen
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27
Q

Protein (apoprotein) + nonprotein (prosthetic group)

A

conjugated proteins

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28
Q

prosthetic group

A
  • lipid (lipoprotein)
  • carbohydrate (glycoprotein)
  • metals (metalloprotein)
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29
Q

types of simple proteins

A

a. globular
b. fibrous

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30
Q

major plasma proteins

A
  1. Pre-albumin
  2. Albumin
  3. Globulins
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31
Q

Migrates ahead of albumin in the classic electrophoresis of serum or plasma proteins

A

Pre-Albumin

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32
Q

Transport of thyroid hormones (thyroxine and triiodothyronine)

A

pre - albumin

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33
Q

binds with retinol-binding protein to form complex that transports retinol (Vitamin A)

A

pre-albumin

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34
Q

rich in tryptophan and contains 0.5% carbohydrate

A

pre-albumin

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35
Q

increased in pre-albumin

A
  • alcoholism
  • chronic renal failure
  • steroid treatment
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36
Q

largest plasma protein fraction

A

albumin

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37
Q

what is the fraction of Albumin

A

52-62%

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38
Q

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

A

albumin

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39
Q

serves as circulating reservoir of AA

A

Albumin

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40
Q

regulator of osmotic pressure (fluid balance)

A

Albumin

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41
Q

Transport protein because of ease of binding with blood components

A

Albumin

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42
Q

indicator of nutritional status

A

albumin

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43
Q

reference values of Albumin

A

3.5 – 5.0 g/dL (35 – 50 g/L)

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44
Q
  • No clinical significance
  • Hemoconcentration, dehydration
  • Excessive albumin infusion
A

Increased Albumin (Hyperalbuminemia)

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45
Q
  • Impaired synthesis (primary= liver disease; secondary = diminished
    protein intake)
  • Decreased synthesis (liver impairment)
  • Malabsorption or malnutrition
  • Nephrotic syndrome (renal loss)
  • Severe burns
A

Decreased Albumin (Hypoalbuminemia)

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46
Q

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

A

Globulins

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47
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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48
Q

Normal A/G ratio

A

1.3-3:1

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49
Q

Low Albumin/Globulin ratio causes

A
  • liver diseases
  • infectious diseases
  • multiple myeloma
  • nephritis
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50
Q

function of a-1-antitrypsin

A

inhibits protease neutrophil elastase

51
Q

neutralize trypsin-like enzymes

A

a-1-antitrypsin

52
Q

Major inhibitor of protease activity; inhibit lysosomal elastase released from PMNs during their response to particles & inhaled bacteria

A

a-1-antitrypsin

53
Q

Most abundant protein in the fetal serum

A

a-1-fetoproteins

54
Q

-Increased in amniotic fluid and maternal serum in
neural tube defects (spina bifida)
* Synthesized initially by the fetal yolk sac & then the
parenchymal cells of the liver

A

a-1-fetoproteins

55
Q

a-1-fetoproteins is detectable in the maternal blood up to the ___ month of pregnancy

A

7th or 8th

56
Q

a-1-fetoprotein peaks in the fetus at ___ weeks of gestation

A

13

57
Q

maternal serum of a-1-fetoprotein increased in the presence of ___

A

twins

58
Q

Diagnostic significance of AFP

A
  • Detects neural tube defects
  • Used as a tumor marker (hepatic & gonadal CA)
  • Screening test for any fetal conditions, increase
    passage of fetal proteins into the amniotic fluid;
    detects neural tube defects
59
Q

increased in AFP

A
  • hepatoma neural tube defects (spina bifida),
  • atresia of the GIT,
  • fetal distress,
  • ataxia telangiectasia,
  • tyrosinosis,
  • hemolytic disease of the newborn (HDN)
60
Q

decreased in AFP

A
  • trisomy 18
  • down syndrome
61
Q

other name for a-1-acid glycoprotein

A

orosomucoid

62
Q

contains high percentage of CHO and sialic acid

A

a-1-acid glycoprotein

63
Q

percentage of CHO in orosomucoid

A

45

64
Q

percentage of sialic acid in orosomucoid

A

11-12

65
Q

Synthesized both by the liver & by granulocytes and
monocytes

A

aag

66
Q

Inhibits the phagocytic activity of neutrophils & inhibits
platelet aggregation

A

aag

67
Q

May inactivate progesterone

A

aag

68
Q

increased in aag( a -1 -acid glycoprotein)

A

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

69
Q

Alpha 2- Globulins

A
  • Haptoglobin
  • Ceruloplasmin
70
Q

the mature haptoglobin is a tetramer; how many chains

A

2a; 2b

71
Q

synthesized in the hepatocytes, an acute-phase protein

A

haptoglobin

72
Q

where is haptoglobin synthesized

A

hepatocytes

73
Q

copper-containing protein BUT does NOT transport
copper; synthesized in the liver, where 6-8 copper
atoms are attached

A

ceruloplasmin

74
Q

how many copper atoms are attached in ceruloplasmin?

A

6-8

75
Q

Imparts a blue color to protein

A

ceruloplasmin

76
Q

marker of wilson’s disease(0.1 g/L ceruloplasmin)

A

ceruloplasmin

77
Q

Copper deposits in the cornea

A

Kayser-Fleischer ring

78
Q

o Upon intake of copper, there is malfunction in the
transport systems within the cell
o No copper being absorbed in the brain, skin and
bones
o Absorbed only in the kidney which is directly
secreted in urine
o Primarily affects male infants

A

Menke’s syndrome

79
Q

menke’s syndrome is also known as

A

Kinky hair disease

80
Q

Carrier for iron (transferrin) and lipids (lipoproteins)

A

Beta Globulins

81
Q

Beta globulins are increased in

A
  • elevated beta lipoprotein (LDL)
  • iron deficiency anemia
82
Q

transferrin is also called as

A

siderophilin

83
Q

A glycoprotein, is a negative acute-phase protein synthesized in the liver

A

tranferrin

84
Q

Functions:
o Transport of iron
o Prevents loss of iron through the kidneys

A

transferrin

85
Q

Tested to determine the cause of anemia, to gauge
iron metabolism, and to determine the iron-carrying
capacity of the blood

A

transferrin

86
Q

increased in siderophilin

A
  • hemochromatosis (bronze skin)
  • Iron deficiency anemia
87
Q

decreased in siderophilin

A
  • liver disease
  • malnutrition
  • nephrotic syndrome
88
Q

Gamma globulins increased in:

A

o Chronic inflammation
o Cirrhosis or viral hepatitis
o Collagen diseases
o Monoclonal gammopathies

88
Q

gamma-globulins

A

o Congenital or acquired immunodeficiency

89
Q

Are 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 (Ab)

90
Q
  • Most abundant Ab found in plasma and lymph
  • Usually fights on bacteria, viruses by agglutination
A

IgG

91
Q
  • Main Ab found in mucous secretions (tears, saliva
    colostrum, vaginal fluid, respiratory and gastrointestinal mucosa secretions)
A

IgA

92
Q
  • First Ab that appears in response to antigenic stimulation
A

IgM

93
Q
  • Present mostly on the surface of B cells and its concentration increased in inflammation, liver
    diseases and connective tissue disorders
A

IgD

94
Q
  • Associated with allergic and anaphylactic reactions,
    parasitism
A

IgE

95
Q
  • One of the largest proteins in blood plasma
  • Synthesized in the liver, and it is classified as a glycoprotein
A

Fibrinogen

96
Q
  • Most abundant coagulation factors
  • An acute phase reactant
A

Fibrinogen

97
Q

Transport cholesterol, triglycerides, and phospholipids in the blood

A

Lipoprotein

98
Q

examples of lipoproteins

A
  • chylomicrons
  • VLDL (Very low density lipoprotein)
  • HDL (High Density Lipoprotein)
  • LDL (Low density lipoprotein)
99
Q

One of the natural defense mechanisms that protects
the human body from infections

A

Complement

100
Q

Participates in the immune reaction and serve as a link to the inflammatory response

A

complement

101
Q

Circulates in the blood as nonfunctional precursors

A

complement

102
Q

most abundant complement protein in the human
serum which is important in the pathogenesis of agerelated macular degeneration

A

C3

103
Q

marker for assessing disease activity in rheumatic
disorders such as Rheumatoid Arthritis (RA) and
Systemic Lupus Erythematosus (SLE)

A

C3 and C4

104
Q
  • It precipitates with the C substance, a polysaccharide
    of pneumococci
  • It may be undetectable in the blood of healthy
    individuals
A

C-reactive protein

105
Q
  • It is a cardiac marker
  • One of the most acute phase proteins that rise in
    response to inflammatory diseases
A

C-reactive protein

106
Q
  • Also used as rapid test for presumptive diagnosis of
    bacterial vs. viral infection
A

C-reactive protein

107
Q

Miscellaneous proteins

A
  • myoglobin
  • troponins
  • amyloid
108
Q

A small heme protein found in skeletal and cardiac
muscles

A

myoglobin

109
Q

When striated muscles are damaged, _____ is
released and it elevates blood levels

A

myoglobin

110
Q
  • Primary oxygen-carrying protein found in striated
    skeletal and cardiac muscle
  • It has a greater affinity for oxygen than does hemoglobin
A

myoglobin

111
Q
  • As a cardiac biomarker, _______ has been used in
    conjunction with troponin to help diagnose or rule out
    a heart attack
  • In Acute Myocardial Infarction (AMI), the onset is 1-3
    hours, peak level 5-12 hours, normalize in 18-30
    hours
A

myoglobin

112
Q
  • Useful marker for monitoring the success of failure of
    reperfusion
A

myoglobin

113
Q
  • A complex of 3 proteins that bind to the thin filaments of striated muscle (cardiac and skeletal)
  • Diagnostic marker for identifying cardiac injury in the presence of skeletal muscle damage
A

troponins

114
Q

Insoluble fibrous protein aggregates formed due to an
alteration in their secondary structure known as β-
pleated sheets

A

amyloid

115
Q

amyloid is Insoluble fibrous protein aggregates formed due to an
alteration in their secondary structure known as ______

A

B-pleated sheets

116
Q

Amyloid is a pathological extracellular deposit associated with group of disorders collectively called ________

A

amyloidosis

117
Q

amyloid stains with what dye?

A

congo red

118
Q

chief nitrogenous macromolecules of cellular structure and organization

A

protein

119
Q

protein composes of ____ of the cell’s dry weight

A

50-70%

120
Q

synthesized in the liver and secreted by the hepatocyte into the circulation except immunoglobulins

A

proteins

121
Q

protein is synthesized in what organ?

A

liver

122
Q

protein is secreted in the_

A

hepatocyte

123
Q

Impaired synthesis (primary= ______; secondary = ______)

A

Liver disease; diminished protein intake