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Lab Diagnosis > Specific Proteins > Flashcards

Specific Proteins Flashcards

1
Q

Separates protein according to their electrical charges (usually at pH 8.6)

A

Protein electrophoresis

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2
Q

Major proteins in plasma that contribute to the electrophoretic pattern are:

A 
Albumin
Alpha1 anti trypsin
Alpha2 macro globulin
Haptoglobin
Beta lipoprotein
Transferrin
Complement C3
Fibrinogen
Immunoglobulin
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3
Q

Plays several roles, including maintaining oncotic pressure, transporting small molecules and promoting or inhibiting inflammatory reactions

A

Plasma proteins

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4
Q

The major clinical of serum and urine protein electrophoresis is to screen for:

A

Monoclonal gammopathies

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5
Q

Methods to quantitate and fractionate proteins:

A 
Turbidimetry
Colorimetry
Absorption spectrophotometry
Dye binding
Column chromatography
Electrophoresis
Immunoassays
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6
Q

Process of unfolding the protein (using heat, pH or chemical compounds)

A

Denaturation

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7
Q

The final shape of protein, has the lowest free energy possible

A

Conformation

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8
Q

Protein shape determined by amino acid sequence

A

Protein folding

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9
Q

Consist of repeating sequence of amino acids

A

Polypeptide backbone

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10
Q

Important numbers: Proteins

A

16% nitrogen which differentiates it from CHO and lipids
15% make up of the cell
20 amino acids linked by peptide bonds

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11
Q

Simple protein: symmetrical, compactly folded polypeptide chains (albumin)

A

Globular

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12
Q

Simple protein: elongated, asymmetrical polypeptide chains (troponin and collagen)

A

Fibrous

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13
Q

Conjugated proteins: with a metal prosthetic group

A

Metalloproteins

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14
Q

Conjugated proteins: lipid prosthetic group

A

Lipoprotein

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15
Q

Conjugated proteins: with 10-40% CHO attachment ( haptoglobin)

A

Glycoproteins

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16
Q

Conjugated proteins: with >40% CHO attached (mucin)

A

Mucoprotein

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17
Q

Conjugated proteins: with DNA or RNA attached (chromatin)

A

Nucleoproteins

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18
Q

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

A

Primary Structure

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19
Q

Hydrogen bonds in peptide backbone; forms alpha and beta pleated sheets

A

Secondary structure

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20
Q

Non covalent interaction; coiled polypeptide chain folds upon itself to form a 3 dimensional structure

A

Tertiary structure

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21
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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22
Q

Separated proteins dissolved in an electrolyte solution by application of an electric current through u shaped quartz tube

A

Electrophoresis

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23
Q

Separation of the protein fractions into discrete bands or zones due to introduction of filter paper as an anti convection support medium

A

Zonal electrophoresis

24
Q

The buffer flow which carries the proteins with mechanical flow, not by charge (agar)

A

Endosmosis/ electro-osmosis

25
Q

Principles of endosmosis/ electro-osmosis

A

Positively charged ion - free to move under electromotive force - flow of buffer towards the CATHODE

Negatively charged ion - tends to move it towards the ANODE

26
Q

Determines the amount of current and the movement of the proteins for a fixed voltage

A

Ionic strength of the buffer

27
Q

Principles of Ionic strength of the buffer:

A

If low, more current is carried by the charged proteins

If high, less current is carried by the proeins, shorter distance reached

28
Q

Support medium for ionic strength:

A

Cellulose acetate membrane
Agarose gel
Starch gel
Polyacrylamide gel

29
Q

Devised to resolve albumin and globulins into 2 or more fractions that can be measured for protein content

A

Precipitation

30
Q

Globulins precipate through addition of:

A

Na sulfate
Na sulfite
ammonium sulfate
Methanol

31
Q

Used extensively as it accentuates abnormalities in serum protein composition, which involves depression of albumin and elevation of more globulin fractions

A

A/G ratio

32
Q

Simplest and mildest of all chromatography techniques, separation is based on differences in size

A

Size exclusion chromatography / SEC

33
Q

Principles of SEC:

A

Size matters: Large proteins will elute first and the smallest ones will elute last

All CHON species continuously move through gel filtration columns all at the same time but at different rates

34
Q

Based on the reversible interaction between a charged protein and an oppositely charged chromatography medium

A

Ion exchanged chromatography (IEC)

35
Q

Proteins are usually applied at basic pH 8.6 at which they may negatively charged or may have no net charge

A

Anion Exchange chromatography

36
Q

Principles of anion exchange chromatography:

A

Neutral CHON pass through an anion exchange column

Anionic proteins stick to the (+) charged column matrix

37
Q

Begins at aid pH, with proteins having positive charge and adhering to a negatively charged column matrix

A

Cation exchange chromatography

38
Q

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

A

Hydrophobic chromatography

39
Q

Specific binding between a protein of interest and another protein that has been covalently linked to a solid support medium of column

A

Affinity chromatography

40
Q

The most common use of affinity chromatography is for:

A

Purification of recombinant proteins

41
Q

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

A

Capillary electrophoresis

42
Q

The ultimate reference method for determining concentration of proteins

A

Nitrogen analysis

43
Q

Consists of acid digestion to release ammonium ions from nitrogen containing compounds

A

Kjeldahl technique ( the reference method)

44
Q

In which double iodides (K and Hg) forms a colored complex with ammonia in an alkali medium

A

Nesslerization

45
Q

Used to estimate specific gravity and by interference, protein content

A

Cooper sulfate solution

46
Q

Protein in solution absorbs ultraviolet light at 280 nm

A

Absorbance

47
Q

Detects turbidity produced by precipitation of a reagent antibody with its target protein in a serum sample

A

Nephelometry

48
Q

Measures major serum proteins in automated immunochemical analyzers

A

Nephelometry

49
Q

Immunologic method that detects proteins in lower concentration

A

radioimmunoassay (RIA) and ELISA

50
Q

Standard dyes for electrophoresis:

A

Coomassie brilliant blue
Ponceau S
Amido black

51
Q

Possible by virtue of the specific binding of albumin to certain dyes. Dyes bound to albumin absorb maximally at slightly different wavelengths

A

Quantification of albumin

52
Q

Dyes used for quantitation of albumin:

A 
Bromphenol blue
Methyl orange
Hydroxybenzenebenzoic acid
Bromcresol purple
Bromcresol green
53
Q

Protein forms precipitate on the addition of trichoroacetic acid and sulfosalicylic acid but not specific to proteins

A

Turbidimetric methods

54
Q

Highly specific for proteins and peptides that uses biuret method in which copper salts in alkaline solution forms a purple complex with substances containing 2 or more peptide bonds

A

Colorimetric technique

55
Q

Oxidizes phenolic compounds so that a greater sensitivity can be obtained giving a deep blue color

A

Folin ciocalteu reagent

56
Q

Uses biuret method plus phenol reagent to enhanced color formation

A

Lowey assay

Lab Diagnosis (7 decks)

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