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Lab Diagnosis > specific proteins > Flashcards

specific proteins Flashcards

1
Q

how many percent of nitrogen is present in protein?

A

16%

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2
Q

protein makes up ___% of the cell

A

15%

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3
Q

proteins are made up of ___ amino acids linked by peptide bonds

A

20

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4
Q

polypeptide backbone is made up of:

A

repeating sequence of amino acids

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5
Q

what determines the protein shape?

A

amino acid sequence

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6
Q

process of unfolding the protein

A

denaturation

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7
Q

Symmetical, compactly folded polypeptide chains

albumin

A

globular proteins

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8
Q

Elongated, asymmetrical polypeptide chains

Troponin & collagen

A

Fibrous

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9
Q

help determine confomation in

aqueous solution.

A

Side chains or R groups

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10
Q

Conjugated Proteins with a metal prosthetic group.

A

metalloprotein

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11
Q

Conjugated Proteins With a lipid prosthetic group.

A

lipoprotein

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12
Q

Conjugated Proteins with 10-40% CHO’s attached (haptoglobin)

A

glycoprotein

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13
Q

Conjugated Proteins with >40% CHO’s attached (Mucin)

A

mucoprotein

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14
Q

Conjugated Proteins with DNA or RNA attached (chromatin)

A

nucleoprotein

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15
Q

The amino acids are linked to each other through covalent peptide
bonding in a specific sequence to form a polypeptide chain

A

Primary Structure

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16
Q

Hydrogen bond in peptide backbone; Polypeptide chain
winds to form alpha helices and beta pleated sheets through
formation of hydrogen bonds.

A

Secondary Structure

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17
Q

Non covalent Interaction; R-groups within protein; Coiled
polypeptide chain folds upon itself to form a 3-dimensional
structure.

A

Tertiary Structure

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18
Q

Two or more folded Polypeptide chains bind to each other
through hydrogen bonds and electrostatic interactions to form
a functional protein

A

Quaternary Structure

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19
Q

Combining all the different side groups and
their different degrees of dissociation, the pH at which a particular protein
has net charge equal to zero is called

A

isoelectric point

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20
Q

proteins are sythesized from___

A

amino end to carboxyl end

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21
Q

The correct assembly of a protein may critically depend

on the function of__

A

molecular chaperones

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22
Q

proteins

that guide the folding of nascent proteins

A

molecular chaperones

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23
Q

consists of the enzymatically regulated attachment of phosphate
groups to serine and threonine groups as well as tyrosine

A

phosphorylation

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24
Q

links glucose to asparagine

A

N-acetylglucosamine

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25
Q

glucose to serine or threonine is linked by

A

N-acetylgalactosamine

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26
Q

results
in the cleavage or removal of short segments of the peptide backbone that
can open up catalytic sites of a zymogen

A

proteolysis

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27
Q

electrophoresis is introduced by

A

Tiselius

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28
Q

He
separated proteins dissolved in an electrolyte solution by application of an
electric current through a U-shaped quartz tube

A

Tiselius

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29
Q

Four serum protein fractions (at 7.6pH) were identified and

quantified optically by change in refractive index

A

albumin, α,

β, and γ,

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30
Q

Introduction of filter paper as an anticonvection support medium permitted
separation of the protein fractions into discrete bands or zones in a
process termed

A

Zonal electrophoresis

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31
Q

it is the result when samples at the center of the gel migrate farther than
those at the edges.

A

smile artifact

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32
Q

After electrophoresis, the gel is treated with

A

mild fixative, such as

acetic acid

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33
Q

are used to generate
tracings and to quantitate the relative percentages of protein in each
fraction.

A

Densitometric scanners

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34
Q

positive pole

A

anode

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35
Q

carries the proteins with it to some extent by mechanical flow, not by
charge.

A

electro-osmosis or endosmosis

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36
Q

is an inert support medium whose porosity is easily

adjusted by changing the composition of acrylamide before polymerization.

A

Polyacrylamide

37
Q

is applicable to
standard separation of native proteins, it can also be used for separating
proteins according to molecular weight when they are denatured in the
presence of sodium dodecyl sulfate (SDS).

A

polyacrylamide gel electrophoresis (PAGE)

38
Q

the
most widely used protein electrophoretic technique for research in molecular
biology.

A

SDS-PAGE

39
Q

uses standard
separation in one direction followed by SDS-PAGE in the perpendicular
direction.

A

two-dimensional electrophoresis (2-DE),

40
Q

devised
to resolve albumin and the globulins into two or more
fractions that can then be measured for protein content.

A

Chemical Precipitation

41
Q

Globulins precipitate through addition of

A

Sodium Sulfate,
Sodium Sulfite
, Ammonium Sulfate &
Methanol.

42
Q

has been
used extensively because it accentuates abnormalities in serum protein composition, which in disease generally involve depression of albumin and
elevation of one or more globulin fractions

A

(A/G ratio)

43
Q

causes of albumin depression

A

-decreased synthesis (malnutrition, malabsorption, liver failure,
diversion to synthesis of other proteins)
- increased loss (proteinuria,
accumulation of ascites fluid, enteropathy).

44
Q

why is precipitation not as accurate as zonal electrophoresis?

A

because some a-globulins don’t precipitate, leading to an overestimate of albumin

45
Q

Gel filtration media

A

Sephadex or agarose

46
Q

Simplest and mildest of all chromatography techniques

 Separates molecules based on differences in size

A

Size-exclusion chromatography (SEC)

47
Q

in this technique, the order of protein

elution is by molecular weight or size, from largest first to smallest last.

A

gel filtration

48
Q

takes advantage of
the charge on proteins to bind them to beads of a support medium with
positively charged components such as diethylaminoethyl or quaternary
aminoethyl.

A

Ion-exchange chromatography

49
Q

proteins are usually
applied at a basic pH such as 8.6, at which they may be negatively charged
(albumin and α1-, α2-, and β-globulins are anions) or may have no net
charge (γ-globulins).

A

anion-exchange chromatography

50
Q

Negatively charged proteins

A

Albumin and α1-, α2-, β-globulins

51
Q

No net charge proteins

A

Υ-globulins

52
Q

begins at an acid pH, with the
proteins having positive charge (cations) and adhering to a negatively
charged column matrix such as carboxymethylcellulose.

A

Cation-exchange chromatography

53
Q

which samples are applied at high salt and are eluted with low salt.
The support medium interacts with proteins with a hydrophobic nature

A

hydrophobic chromatography

54
Q

is based on specific binding between a protein
of interest and another protein that has been covalently linked to the solid
support medium of a column.

A

affinity chromatography

55
Q

the most common use of affinity chromatography

A

purification of recombinant proteins

56
Q

is a separation method based on flow through
a capillary tube that can be tailored to resolution of different molecules
based on size, hydrophobicity, or stereospecificity

A

Capillary electrophoresis

57
Q

capillary electrophoresis is applicable to

A

DNA or proteins, as well as to small ones such as hormones

or therapeutic drugs

58
Q 
the method is similar to highperformance
liquid chromatography (HPLC),
A

Capillary electrophoresis

59
Q

The ultimate reference method for determining concentration of protein
is

A

nitrogen analysis

60
Q

consists of acid

digestion to release ammonium ions from nitrogen-containing compounds.

A

Kjeldahl technique

61
Q 
double iodides (potassium
and mercuric) form a colored complex with ammonia in alkali.
A

nesslerization

62
Q

can be accurate for measuring serum protein concentration

as dissolved solute for levels above 2.5 g/dL.

A

Refractive index

63
Q

can be estimated
by pipetting drops of serum or blood into a graded series of copper
sulfate solutions

A

Specific gravity

64
Q

This technique is simple
and has been used widely as a screening test for hemoglobin concentration
in whole blood.

A

Copper Sulfate Solution technique

65
Q

Proteins in solution absorb ultraviolet light at

A

280 nm (A280),

66
Q

amino acids the commonly absorb UV light

A

tryptophan, tyrosine and phenylalanine

67
Q

can be used for quantitating proteins

in the range of 0.05–1.5 mg/mL.

A

Direct measurements of absorbance

68
Q

are often used for a similar concentration range

in CSF or urine.

A

Turbidimetric methods

69
Q

in turbidimetric methods, Protein forms precipitate on the addition of

A

trichloroacetic

acid, sulfosalicylic acid, or other acid reagent.

70
Q

a type of calorimetric techinque highly specific for proteins and peptides

A

Biuret method

71
Q

copper salts in alkaline solution form a purple

complex with substances containing two or more peptide bonds.

A

Biuret method

72
Q

reagent which oxidizes phenolic
compounds such as tyrosine and, in addition, tryptophan and histidine
to give a deep blue color.

A

Folin-Ciocalteu reagent

(or phenol reagent, phosphotungstomolybdic acid),

73
Q

used the Biuret method followed by the phenol reagent,
which greatly enhanced color formation, because the phenol reagent can
react with Biuret complexes involving all peptide bonds.

A

.Lowry

74
Q

is extensively used in clinical
laboratories, particularly in automated analyzers in which protein concentration
can be measured down to 10 or 15 mg/dL.

A

Biuret method

75
Q

has been extensively used for consistently accurate determinations of
protein concentration.

A

Lowry assay

76
Q

Further sensitivity for detection down to 1 μg of protein can be
obtained using

A

Coomassie brilliant blue dye

77
Q

develops a

violet color by reacting with primary amines.

A

ninhydrin

78
Q

This reagent is widely used
for detection of peptides and amino acids after paper chromatogaphy and
amino acid analyses from ion-exchange columns, as well as for detection
of drugs on toxicology screens using thin-layer chromatography

A

ninhydrin

79
Q

Quantitation of albumin in the presence of other proteins is possible
by virtue of the specific binding of albumin to certain dyes such as

A 
bromphenol blue
 methyl orange
 hydroxybenzeneazobenzoic acid
bromcresol purple
 bromcresol green (BCG).
80
Q

used extensively in automatic
analyzers for determining serum albumin in parallel with Biuret
reagent for total protein.

A

BCG

81
Q

The standard dyes used for staining electrophoresis

A

Coomassie

brilliant blue, Ponceau S, and amido black.

82
Q

used For detection of minor components
in high-resolution gels very sensitive down to
nanogram quantities

A

silver staining

83
Q

stain

lipoproteins

A

Oil Red O and Sudan black

84
Q

stains glycoproteins

A

periodic acid–Schiff

85
Q

detects the turbidity produced usually within minutes or less by
the precipitation of a reagent antibody with its target protein in a serum
sample

A

Nephelometry

86
Q

The major serum proteins are now widely measured

by this method on automated immunochemistry analyzers

A

Nephelometry

87
Q

Proteins
present in lower concentrations may be quantitated by immunologic
methods, such as

A

radioimmunoassay (RIA) or enzyme-linked immunosorbent

assay.

88
Q

those components that are readily resolved
and detected on electrophoretic gels stained by conventional clinical laboratory
techniques

A

major serum proteins

Lab Diagnosis (2 decks)

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