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CYTOGEN > TECHNIQUES IN PROTEIN ANALYSIS > Flashcards

TECHNIQUES IN PROTEIN ANALYSIS Flashcards

1
Q

it is the most abundant macromolecules in biological system.

A

Proteins

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2
Q

They are polymers comprising amino acids that are linked by peptide bonds.

A

Proteins

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3
Q

These proteins can be detected in the blood of the patient which are considered as __________

A

Biomarkers

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4
Q

it is a measurable substance in the blood whose presence is indicative of diseases or environmental exposure

A

biomarkers

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5
Q

it is the most common method for purifying proteins from other protein molecules with a given sample

A

Column Chromatography

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6
Q

it involves the separation of soluble components in a solution by specific differences in physical-chemical characteristics of the different constituents

A

Column Chromatography

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7
Q

True or False:
Small molecules are more likely to go through the pore of the matrix. They are trapped inside the resin and will travel through the column more slowly.

A

True

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8
Q

True or False:
Large molecules move through the column more quickly

A

True

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9
Q

This type of column chromatography has many tiny pores in the resin bead.

A

Gel/ Gel Permeation/ Gel Filtration/ Size Exclusion

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10
Q

This type of column chromatography uses resin to separate proteins according to their surface charges

A

Ion Exchange Chromatography

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11
Q

It contains a resin bearing either positively or negatively charged chemical groups.

A

Ion Exchange Chromatography

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12
Q

True or False:
In Ion Exchange Chromatography, the resins with positively charged groups (anion-exchange resins) attract negatively charged solute.

A

True

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13
Q

True or False:
In Ion Exchange Chromatography, Opposite charges attract. - It traps (-) charged molecules so (+) charged
molecules are first obtained.

A

True

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14
Q

This type of chromatography uses the so called lock and key binding that is widely present in biological system.

A

Affinity Chromatography

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14
Q

It is used to separate and prepare larger quantities of proteins and antibodies for study.

A

Affinity Chromatography

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14
Q

This type of Column Chromatography It uses the principle that the protein binds to a
molecules for which it has specific affinity.

A

Affinity Chromatography

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15
Q

This technique has different purposes: : for separation, to determine the sizes, presence, or amount of DNA

A

Electrophoresis

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16
Q

We use this kind of gel electrophoresis for proteins

A

Polyacrylamide gel electrophoresis with SDS

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17
Q

It is carried out with a stacking gel and separating gel

A

Polyacrylamide gel electrophoresis with SDS

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18
Q

This technique associated with staining method can detect bands of protein in a simple and relatively rapid manner.

A

Electrophoresis

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19
Q

SDS-PAGE meaning

A

Sodium Dodecyl Sulphate Polyacrylamide gel electrophoresis

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20
Q

True or False:
Sodium Dodecyl Sulphate Polyacrylamide gel electrophoresis is an anionic detergent (-)

A

True

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21
Q

It disrupts the structure of protein to be linear and binds most protein

A

Sodium Dodecyl Sulphate

22
Q

These agents break the covalent bonds that are present

A

dithiothreitol (DTT) or 2-
mercaptoethanol

23
Q

Advantages of SDS

A

it coats all the polypeptides with negative charges

It masks the natural charges of the subunit

24
Q

What are the two types of staining methods

A

Colorimetric and Fluorescence

25
Q

Give the 3 high sensitivity colorimetric staining methods that can be used either directly after electrophoresis

A

Coomassie blue staining, zinc-reverse staining, and silver staining

26
Q

It is one of the 3 high sensitivity colorimetric that is most frequently employed method for protein detection in SDS-PAGE gel

A

Coomassie blue staining

27
Q

It is one of the 3 high sensitivity colorimetric that Uses imidazole and zinc salts for protein
detection in electrophoresis gels

A

Zinc-reverse staining/ Negative Staining

28
Q

It is one of the 3 high sensitivity colorimetric that is based on the binding of silver ions to the
proteins followed by reduction to free silver, sensitization, and enhancement

A

Silver staining

29
Q

This dye give very wide linear dynamic ranges, over four orders of magnitude.

A

Fluorescence dye

30
Q

Although this type of dye can even reveal as low as 1 ng of protein, it is inconvenience because it has
to be incorporated before gel electrophoresis.

A

CyeDyes

31
Q

It is a better resolving power as compared to the SDSPAGE, especially if there is a mixture of polypeptides or when it’s too complex

A

Two-dimensional Gel Electrophoresis

32
Q

the complex protein samples are
separated in two dimensions according to their net charge at different pH and their molecular
weights determined by SDS-PAGE.

A

Two-dimensional Gel electrophoresis

33
Q

In this dimension, the . Sample is placed in a narrow tube gel or subjected to isoelectric focusing
based on pH.

A

First Dimension

34
Q

In this dimension, the strip is placed at the top of the SDS-PAGE.

A

Second dimension

35
Q

It is another method related to gel electrophoresis that is used to detect specific protein molecules from among a mixture of proteins

A

Western Blot

36
Q

This blot is used to detects the RNA

A

Northern blot

37
Q

This blot is used to detects the DNA

A

Southern blot

38
Q

This blot is used to detects the Proteins

A

Western blot

39
Q

3 elements used in western blot

A
  1. Separation by size.
  2. Transfer to a solid support.
  3. Use a specific or proper primary and secondary antibody for visualization.
39
Q

It is a method of transferring protein onto membranes that is aided by capillary action (by placing a weight on the gel and membrane) or vacuum (for faster and more uniform transfer)

A

diffusion/ passive transfer

40
Q

It is achieved by posing a membrane sheet on one or both side of the gel

A

diffusion/ passive transfer

41
Q

This method of transferring protein onto membranes are driven by an electrical field and is achieved by putting a gel membrane in a
suitable holder and immersing both the gel and membrane in a tank filled with buffer fitted
with two plate electrode (+ and -)

A

electroblotting/ electrotransfer

42
Q

This method of transferring protein can use spectrophotometer in detecting proteins

A

UV Absorption Method

43
Q

A common laboratory technique which is used to measure the concentration of an analyte in a solution

A

ELISA

44
Q

It is a quantitative immunological procedure in which antigen-antibody reaction is monitored by
enzyme measurement.

A

ELISA

45
Q

This assay uses the coupling of antigens and antibodies and relies on the specificity and affinity of antibodies for antigens.

A

ELISA

46
Q

It uses a primary labeled antibody that react directly with the antigen

A

DIRECT ELISA

47
Q

It can be performed with the antigen that is directly immobilized on assay plate.

A

DIRECT ELISA

48
Q

it uses only an enzyme-labelled
primary antibody. The secondary antibodies are not needed.

A

DIRECT ELISA

49
Q

It utilizes a primary unlabeled antibody in conjunction with a labeled secondary antibody

A

INDIRECT ELISA

50
Q

both primary and secondary
antibody are used, but in this case, the primary antibody is not labelled (no enzyme-linked). The enzyme is labelled with the secondary
antibody.

A

INDIRECT ELISA

51
Q

Antigens like Tumor markers, hormones, serum proteins may be determined.

A

SANDWICH ELISA

52
Q

In this type of ELISA, you need to prepare a surface to which a known quantity of antibody is bound.

A

SANDWICH ELISA

53
Q

it is Used to determine the precise mass of peptides.

A

MALDI-TOF

54
Q

IT is a very sensitive and accurate for determining amino acid sequences.

A

MALDI-TOF

CYTOGEN (11 decks)

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