Protein Flashcards

1
Q

has 2 differing charges

A

Zwitterion

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2
Q

Proteins differ in their pI values, but for most proteins it
occurs in the pH range of

A

5.5 to 8

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3
Q

are those that generate
precursors of glucose such as pyruvate or citric acid
cycle intermediates.

A

Glucogenic amino acid

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4
Q

are degraded to acetyl-CoA
such as leucine or lysine.

A

Ketogenic amino acid

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5
Q

PLASMA PROTEINS

A

Albumin
Globulin
Fibrinogen

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6
Q

It serves as transport protein for T4 and retinol (vitamin A) - by complexing with retinol-binding
protein.

A

Pre albumin (transthyretin)

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7
Q

It migrates ahead of albumin.

A

Pre albumin

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8
Q

It has considerable ß-pleated sheet conformation.

A

Pre albumin

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9
Q

Marker of malnutrition

A

Pre albumin

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10
Q

It is the most abundant protein in the
plasma

A

Albumin

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11
Q

It is the protein present in highest concentration in plasma It is synthesized
in the liver.

A

Albumin

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12
Q

Dye Binding methods for albumin measurements employ (most sensitive)

A

Bromcresol green

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13
Q

It serves as circulating reservoir of amino acids.

A

Albumin

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14
Q

Negative acute phase reactant

A

Albumin
Pre albumin
Transferrin

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15
Q

It neutralizes trypsin-like enzymes (like neutrophil elastase) - this enzyme is released
from WBCs to combat infection but it can also destroy alveoli which can lead to
emphysema.

A

A1 antitrypsin

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16
Q

Most abundant protein in fetal serum

A

A-fetoprotein

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17
Q

It is a glycoprotein; migrates between albumin and a-1 globulin band.

A

A-fetoprotein

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18
Q

Maternal serum importance: a fetoprotein

A

Neural tube defect

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19
Q

It has greatest affinity for progesterone; binds quinidine (cardioactive drug).

A

A1-ACID GLYCOPROTEIN

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20
Q

It can be determine in pregnancy

A

A1 - acid glycoprotein

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21
Q

Most abundant fraction PSA

A

A1 - antichymotrypsin

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22
Q

Component of amyloid alzhemers disease

A

A1 -antichymotrypsin

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23
Q

It binds heme released by degradation of
hemoglobin - has the strongest affinity for heme.

A

Hemopexin

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24
Q

it exhibits affinity with vitamin D and actin (vitamin
D- binding protein).

A

Group specific component globulin

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25
Q

It binds free hemoglobin by its a chain.

A

Haptoglobin

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26
Q

presence of hemoglobin

A

Black water fever

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27
Q

Copper binding protein

A

Ceruloplasmin

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28
Q

is a marker for Wilson’s disease

A

Ceruloplasmin

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29
Q

It is the largest major nonimmunoglobulin protein in plasma.

A

A2-macroglobulin

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30
Q

Marker of kidney disorders

A

A2-macroglobulin

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31
Q

Major inhibitor protease

A

A2-macroglobulin

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32
Q

is found on the surface of most nucleated cells; present in high concentration on
lymphocytes.

A

B2-microglobulin

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33
Q

It is needed in the production of CD8 cells.

A

B2-microglobulin

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34
Q

It is a major component of the B2-globulin fraction (electrophoresis).

A

Transferrin

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35
Q

❑It is a glycoprotein, synthesized in the liver; also a negative acute phase
reactant.

A

Transferrin

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36
Q

It is used to determine the cause of anemia, to measure iron metabolism and
determine the iron-carrying capacity of the blood.

A

Transferrin

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37
Q

is the most abundant antibody found in plasma and
lymph

A

Immunoglobulin G

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38
Q

is present mostly on the surface of B cells

A

Immunoglobulin D

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39
Q

is antibody associated with allergic and
anaphylactic reactions.

A

Immunoglobulin E

40
Q

it binds with proteins and lipids forming LDL, HDL,
VLDL and chylomicrons.

A

Lipoprotein

41
Q

is the main antibody found in mucous secretions

A

Immunoglobulin A

42
Q

is the first antibody that appears in response to
antigenic stimulation

A

Immunoglobulin M

43
Q

one of the acute-phase reactants - markedly increased in inflammatory process.

A

Fibrinogen

44
Q

is the most abundant form in serum

A

Complement C3

45
Q

concentration is a convenient marker for assessing disease activity in
rheumatic disorders such as RA and SLE.

A

C3 and C4

46
Q

Heart protein

A

Myoglobin

47
Q

Primary oxygen carrying protein

A

Myoglobin

48
Q

gold standard in myocardial

A

Troponin I

49
Q

MARKER FOR CARDIAC INJURY

A

Troponin

50
Q

Marker of congestive heart failure

A

B-TYPE NATRIURETIC PEPTIDE

51
Q

It is a low molecular weight protein and a cysteine proteinase inhibitor.

A

Cystatin c

52
Q

Hard to measure

A

Cystatin c

53
Q

A fat hormone composed of an N-terminal collagen-like
domain and a C-terminal globular domain produced by
ADIPOCYTES

A

Adiponectin

54
Q

MarkersPremature delivery

A

Fibronectin

55
Q

Kidney problem

A

B-trace protein

56
Q

marker in detecting impaired renal
function

A

B-trace protein

57
Q

marker of bone resumption

A

Cross linked c telopeptides

58
Q

Secondary stucture b pleated sheet

A

Amyloid

59
Q

Microalbuminuria ref value

A

30-300 ug/mg creatinine

60
Q

Clinical albuminuria ref value

A

> 300 ug/mg creatinine

61
Q

Method with peptide bond

A

Buiret

62
Q

It is an inborn error of metabolism characterized
by the absence of homogentisate oxidase in the
tyrosine pathway.

A

Alkaptonuria

63
Q

most sensitive marker of urinary protein (folin phenol- blue) level of amino acid

A

Folin lowy

64
Q

is characterized by markedly reduced or absence of a-ketoacid decarboxylase.

A

Maple syrup urine disease

65
Q

is an autosomal recessive trait characterized by the deficiency of the
enzyme phenylalanine hydrolase (PAH)/phenylalanine-4-mono-
oxygenase, which catalyzes the conversion of phenylalanine to tyrosine.

A

Phenylketonuria

66
Q

Odor of phenylketonuria

A

Mousy odor

67
Q

tyrosinemia I enzymes

A

Fumarylacetoacetate FAA hydrolase

68
Q

Tyrosinemia II enzymes

A

Tyrosine aminotransferase

69
Q

Tyrosinemia III

A

4-hydroxyphenylpyruvic acid oxidase

70
Q

Lost of protein in urine

A

Hydroproteinemia

71
Q

the result of the underlying cause, dehydration.

A

Hyperproteinemia

72
Q

TOTAL NITROGEN method used

A

Kjeldahl method

73
Q

Not used method in the clinical laboratory (time consuming)

A

Kjeldahl method

74
Q

is the most widely used method and the one
recommended for the determination of total protein

A

Buiret

75
Q

are based on the ability of most
proteins in serum to bind dyes

A

Dye binding

76
Q

Digestion of protein; measurement of
nitrogen content

A

Kjeldahl

77
Q

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

A

Buiret

78
Q

is a process wherein filter paper is used as an anticonvection
support medium thus permitting separation of the protein fractions
into discrete bands or zones.

A

Zonal electrophoresis

79
Q

STANDARD DYES USED IN ELECTROPHORESIS
a. For serum protein electrophoresis

A

➢Coomasie Brilliant Blue
➢Ponceau S
➢Amido Black

80
Q

STANDARD DYES USED IN ELECTROPHORESIS For lipoprotteins

A

Sudan black
Oil red o

81
Q

STANDARD DYES USED IN ELECTROPHORESIS For glycoproteins

A

Periodic add schiff

82
Q

It is based on the charge of proteins which binds to
heads of a charged support medium.

A

Ion exchange chromatography

83
Q

fastest band - most anodal protein

A

Albumin 1 band

84
Q

glycoproteins, AAT, AAG,
thyroxine binding-globulin (TBG). It increases as a non-specific
response to inflammation.

A

Alpha 1 globulin (2 fast band)

85
Q

haptoglobin, AMG,
ceruloplasmin

A

Alpha 2 globulin (3 fast band)

86
Q

transferrin, beta-lipoprotein,
hemopexin, complement (C3 and C4), CRP

A

Beta globulin (4band)

87
Q

immunoglobulin

A

Gamma-globulin (5 band; slow band)

88
Q

Gamma spike:

A

Multiple Myeloma

89
Q

Beta-gamma bridging:

A

Hepatic cirrhosis

90
Q

a2-globulin band spike:

A

Nephrotic syndrome

91
Q

a1-globulin flat curve:

A

Juvenile cirrhosis

92
Q

Spikes of a1, a2 and B globulin bands -

A

Inflammation

93
Q

It is the hereditary absence of albumin or inability to
synthesize albumin.

A

Analbuminemia

94
Q

Albumin/Globulin ratio

A

1.3-3:1

95
Q

It is the presence of two albumin bands instead of a single
band in electrophoresis.

A

Bisalbuminemia