Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

LAB DIAG > M1: Specific Protein I > Flashcards

M1: Specific Protein I Flashcards

0
Q

Make up 15% of the cell. Function as enzyme, transporter, structural support, motor function, storage, signaling(pathway receptors), receptors, gene regulation and other special functions.

A

Protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
1
Q

Specific Proteins

A

Globulin, Albumin & Creatinine “GAC”

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Shape of proteins are from

A

AA sequence

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Transporters

A

Apolipoproteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

All enzymes are protein but not all proteins are enzyme. T/F

A

False

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Proteins are made of _____ AAs linked by __________, polypeptide backbone. Consist of repeating sequence of AA. R group/side group/side chain not part of the backbone.

A
  1. Peptide bonds.
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Polar

A

Hydrophilic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Nonpolar

A

Hydrophobic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Determining factor as to chemical nature of proteins

A

Side chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Peptide bind allow for rotation around it

A

Protein folding

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Protein can fold and orient the _______ in favorable positions linked by weak non covalent interactions.

A

R groups

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Weak non covalent interactions

A

Hydrogen bond, Ionic bond & Van der Waals attraction “HIV”

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Side chain/R groups help determine conformation in aqueous solution

A

Globular proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Protein shape determined by

A

AA sequence

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Final shape. Has the lowest free energy possible

A

Conformation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Process of unfolding the protein. Can be done with heat, PH& chemical compound.

A

Denaturation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Folds back on itself as a ribbon (globular protein-muscle)

A

B-pleated sheet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Type of B pleated: run in the same direction

A

Parallel

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Type of B pleated: runs in the opposite direction of its neighbor

A

Antiparallel

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Protein turns like spiral. Fibrous proteins (hairs, nails & horns)

A

A-helix

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Non covalent interaction. R groups within protein.

A

Tertiary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

AA sequence of protein

A

Primary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Two polypeptides

A

Quaternary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Hydrogen bond in peptide chain backbone

A

Secondary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Blood serum is placed into a gel or into liquid in a capillary tube, and exposed to am electric current to separate the serum protein components.

A

Electrophoresi

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

In Electrophoresis, _____ serum protein fractions (at ____pH) were identified and quantified optically by change in _________. albumin, a, B & y.

A

Four. 7.6 Refractive index

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

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

A

Tiselius

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

Separation of the protein fractions into discrete bands or zones d/t the introduction of filter paper as an anticonvection support medium.

A

Zonal Electrophoresis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

In zonal electrophoresis, on solid support medium and at pH of _____, the a fraction further splits into two groups of proteins, a1 & a2.

A

8.6

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

The buffer flow which carries the proteins with it by mechanical flow not by charge. Ex is Agar.

A

Endosmosis/Electro osmosis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

Electrophoresis Principle: are free to move under the electromotive force, and net result is flow of buffer toward the _________.

A

Positively charged ion. Cathode.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

Electrophoresis Principle: the electromotive force to which it is subjected tends to move it toward the _______.

A

Negatively charged ion. Anode.

32
Q

Determines the amount of current and movement of the proteins for a fixed voltage. If the electrodes are not properly aligned, the current may be denser on one side of the gel than the other; proteins will migrate farther on the side with more current.

A

Ionic Strength of the Buffer

33
Q

Ionic Strength of the Buffer: If ____, less current is carried by the proteins, which move a shorter distance.

A

High

34
Q

Ionic Strength of the Buffer: If _____, relatively more current is carried by the charged proteins.

A

Low

35
Q

Rate of migration factors: _______ on the particle.

A

Net charge

36
Q

Rate of migration factors: ______ & ______ of the particles.

A

Mass. Shape.

37
Q

Rate of migration factors: ____ & ____ of the medium

A

pH & Temperature

38
Q

Rate of migration factors: ______ of the electric field(buffer system)

A

Strength

39
Q

Rate of migration factors: _______ of supporting medium

A

Properties

40
Q

Support media

A

Polyacrylamide gel, Agarose gel, Cellulose acetate membrane & Starch gel “PACS”

41
Q

Have predominated in the clinical laboratory because of the ease of use, low cost and commercial availability.

A

Cellulose acetate & Agarose

42
Q

Have been devised to resolve albumin and the globulins into two or more fractions that can then be measured for protein content. Measure total proteins in the original serum & protein in the precipitate or the supernatant, values for albumin & globulin can be derived.

A

Precipitation

43
Q

Globulins can precipitate through the addition of

A

Methanol, Aluminum Sulfate, Sodium Sulfite & Sodium Sulfate “MASS”

44
Q

Precipitation: the ration of these values (______) has been used extensively because it accentuates abnormalities in serum protein composition, which generally involve depression of _______ and more elevation of _______ fractions.

A

A/G ration. Albumin. Globulin.

45
Q

May be depressed owing to decrease synthesis (malnutrition, malabsorption, liver failure, diversion of synthesis to other proteins) and increased loss (proteinuria, accumulation of ascites fluid & enteropathy)

A

Albumin

46
Q

Precipitation methods are not as accurate as zonal electrophoresis, because some _________ may fail to precipitate, thus leading to an overestimate of the albumin fraction.

A

Alpha globulins

47
Q

Simplest & mildest of all chromatography (column separation) Separates molecules based in difference in size.

A

Gel Filtration

48
Q

In Gel Filtration, Particles the size of dissolved salt penetrate farthest into the anterior to the GF beads and come out after all the proteins have emerged in amount of applied buffer called ________.

A

Salt volume

49
Q

Gel Filtration: _______ doesn’t enter gel pores and elute rapidly from the column in the void volume.

A

Large proteins

50
Q

Gel Filtration: _________ repeatedly enter and leave pores of the gel thus remain longer in the column.

A

Smaller proteins

51
Q

Gel Filtration: All protein species continuously move through a gel filtration column all at the same ______ but at different ______.

A

Time. Rates.

52
Q

Gel Filtration: A sample of proteins passing through a gel filtration column will separate based on _________. The big ones will elute ____ and smallest one will elute _____. And middle sized in the middle.

A

Molecular size. First. Last.

53
Q

Based on the reversible interaction between a charged protein and an oppositely charged chromatography medium. Retains analyte molecules on the column based on coulombic(ionic) interactions. Advantage is that biomolecules with even small differences in net surface charge can be separated.

A

Ion Exchange Chromatography

54
Q

Ion Exchange Chromatography: displays ionic functional groups interact with analyte ions of opposite charge. Further subdivided into cation exchange and anion exchange chromatography.

A

Stationary phase surface

55
Q

Keep positively charged cations and shows negatively charged

A

Cation Exchange Chromatography

56
Q

Proteins are usually applied at a basic pH(8.6) Either negatively charged. Neutral proteins pass through an anion exchange column. Anionic proteins stick to the (+) charged column matrix.

A

Anion Exchange Chromatography

57
Q

Anion Exchange Chromatography: are considered as anions

A

Albumin, A1, A2 & B globulins

58
Q

Anion Exchange Chromatography: No net charge

A

Y globulins

59
Q

Samples are applied at high salt; eluted with low salt. The support medium interacts with proteins with a hydrophobic nature.

A

Hydrophobic Chromatography

60
Q

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

61
Q

The most common use affinity chromatography is for the

A

Purification of recombinant proteins

62
Q

Based on a flow through a capillary tube. Can be tailored to resolution of different molecules based on size, hydrophobicity or stereospecificity. Applicable to large & small molecules. Similar to HPLC. Employs column with similar agarose. A detector at the effluent and detects & quantities protein bands. Equipment costs relatively high, reagent labor low costs, fast and very quantitative.

A

Capillary Electrophoresis

63
Q

Solvent is pumped through a column that retains/passes solutes according to chemical interactions

A

High Performance Liquid Chromatography (HPLC)

64
Q

Very basic. Ultimate reference method for determining concentration of proteins. Has the basic principle.

A

Nitrogen Analysis

65
Q

Acid digestion release of ammonium ions. Forms a nitrogen containing compound. Highly accurate but not commonly used in the lab.

A

Kjeldahl Technique

66
Q

Wherein double iodides (potassium & mercuric) forms a colored complex with ammonia in an alkali medium

A

Nesslerization

67
Q

Kjeldahl Technique: ammonium is quantitated by conversion into _________ and titration as a base or by nesslerization.

A

Ammonia gas

68
Q

Used to estimate specific gravity and by inference protein as well. Pipette drops of serum/blood into a graded series of this.

A

Copper sulfate solution

69
Q

Protein concentration is estimated from the __________ of the copper sulfate solution in which the drop remains stationary.

A

Specific gravity

70
Q

Forms to prevent dissolution as a drop falls to the bottom and remains stationary or rises to the top

A

Copper sulfate capsule

71
Q

Protein in a solution absorbs ultraviolet light at 280nm

A

Absorbance

72
Q

Measurement of turbidity. Protein forms a precipitate on the addition of ______________. Not specific for protein. Could be used to measure nucleic acids as well.

A

Turbidimetric Methods. Trichloroacetic/Sulfosalycilic Acids.

73
Q

Highly specific for proteins and peptide. Biuret method. Copper salts in alkaline solution forms a purple complex with substances containing 2 or more peptide bonds. Extensively used among automated laboratories. Ex is chemistry analyzer.

A

Colorimetric Method

74
Q

Used the Biuret method plus phenol reagent equals greatly enhanced color formation. Used for consistently accurate determination of protein concentration.

A

Lowry Assay

75
Q

Reacts with the Biuret complexes involving all peptide bonds

A

Phenol

76
Q

Standard dyes for Electrophoresis

A

Ponceau S, Amido black & Coomasie Brilliant Blue “PAC”

77
Q

Detects turbidity produced by precipitation of a reagent antibody with its target protein in serum sample. Method used for measuring major serum proteins in automated immunochemical analyzers.

A

Nephelometry

78
Q

Immunologic method that detects proteins in lower concentration

A

Radioimmunoassay(RAI) & Enzyme-linked Immunosorbent Assay(ELISA)

LAB DIAG (6 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions