Ch 4 Flashcards

1
Q

the migration of charged solutes or particles in an electrical field.

A

Electrophoresis

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2
Q

refers to the migration of small ions

A

Iontophoresis

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3
Q

is the migration of charged macromolecules in a porous support medium such as paper, cellulose acetate, or agarose gel film

A

Zone Electrophoresis

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4
Q

film is soaked in buffer, the air spaces fill with electrolyte and the film becomes pliable.

A

Cellulose acetate

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5
Q

another widely used supporting medium. Used as a purified fraction of agar, it is neutral and, therefore, does not produce electroendosmosis

A

Agarose Gel

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6
Q

-involves separation of protein on the basis of charge and molecular size. Separates serum proteins into 20 or more fractions rather than the usual 6 fractions separated by cellulose acetate or agarose. It is widely used to study individual proteins

A

Polyacrylamide Gel

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7
Q

separates proteins on the basis of surface charge and molecular size, as does polyacrylamide gel. The procedure is not widely used because of technical difficulty in preparing the gel.

A

Starch gel

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8
Q

The movement of buffer ions and solvent relative to the fixed support is called

A

Endosmosis or Electroendosmosis

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9
Q

Charged proteins migrate through a support medium that has a continuous pH gradient.

A

Isoelectric focusing

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10
Q

is used in the clinical laboratory to characterize monoclonal proteins in
serum, urine, or cerebrospinal fluid (CSF).

A

Immunofixation electrophoresis

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11
Q

separation is performed in narrow-bore, fused silica capillaries (inner diameter 25 to 75 um).

A

Capillary electrophoresis

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12
Q

is the bulk flow of liquid toward the cathode upon application of an electric field, and it is superimposed on electrophoretic migration

A

Electroosmotic Flow (EOF)

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13
Q

This electrophoresis assay combines two different electrophoresis dimensions to separate proteins from complex matrices such as serum or tissue.

A

Two-Dimensional Electrophoresis

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14
Q

is the principle of measuring the concentration of solute particles in a solution using one of the four colligative properties discussed below

A

Osmometry

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15
Q

enables the study of the binding of ligands to surface receptors such as membrane proteins in real time.

A

Surface plasmon resonance

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16
Q

a similar label-free technique that uses sensor tips instead of a flat metal surface.

A

Biolayer interferometry

17
Q

refers to the group of techniques used to separate complex mixtures on the basis of different physical interactions between the individual compounds and the stationary phase of the system

A

Chromatography

18
Q

also known as liquid- solid chromatography, is based on the competition between the sample and the mobile phase for adsorption sites on the solid stationary phase.

A

Adsorption

19
Q

also referred to as liquid- liquid chromatography. Separation of solute is based on relative solubility in an organic (nonpolar) solvent and an aqueous (polar) solvent. In its simplest form, it is performed in a separatory funnel

A

Partition

20
Q

a variation of liquid-solid chromatography, is used to separate solute molecules on the basis of size and shape. The chromatographic column is packed with porous material

A

Steric exclusion

21
Q

used to remove interfering substances from a solution, to concentrate dilute ion solutions, and to separate mixtures of charged molecules, such as amino acids. Changing pH and ionic concentration of the mobile phase allows

A

Ion exchange chromatography

22
Q

a variant of column chromatography. A thin layer of sorbent, such as alumina, silica gel, cellulose, or cross-linked dextran, is uniformly coated on a glass or plastic plate.

It is most commonly used as a semiquantitative screening test.

A

Thin-Layer Chromatography

23
Q

uses pressure for fast separations, controlled temperature, inline detectors, and gradient elution techniques.

A

High Performance Liquid Chromatography (HPLC)

24
Q

forces the mobile phase through the column at a much greater velocity than that accomplished by gravity flow columns and includes pneumatic, syringe, reciprocating, or hydraulic amplifier pumps.

A

Pumps

25
Q

The most common material used for column packing

A

Silica gel

26
Q

used to separate mixtures of compounds that are volatile or can be made volatile.

A

Gas chromatography

27
Q

The column effluent is fed into a small hydrogen flame burning in excess air or atmospheric oxygen.

A

Flame ionization detectors

28
Q

The most common form of ionization used in GC/MS. This method requires a source of electrons in the form of a filament to which an electric potential is applied, typically at 70 eV.

A

Electron ionization

29
Q

ionization is used for the analysis of biomolecules such as peptides and proteins.

A

Time of Flight (MALDI)

30
Q

are widely used for measuring drugs of abuse in urine toxicology confirmations. Drugs and metabolites must be extracted from body fluids

A

GC/MS