Module 2 Quiz

A  0.065 g/dL

B  15.4 g/dL

C  Albumin values cannot be calculated using densitometry.

D  4.68 g/dL

A  Ion-selective electrode

B  Coulometric method

C  Amperometric method

D  Conductivity-based measurement

A  a lower energy.

B  a higher energy.

C  the same wavelength.

D  a shorter wavelength.

A  a biologic recognition element and a physicochemical transducer, often an electrochemical or optical device.

B  two inert metal electrodes to which an electrical potential is applied.

C  a polarizable working electrode to which an external voltage is applied with the resulting cathodic or anodic current of the cell being monitored.

D  two electron or metallic conducting electrodes that are connected by an electrolyte solution that conducts ions.

A  more efficient heat dissipation for better separation.

B  the small sample size required.

C  the increased amount of time required for separation.

D  the ability to use a variety of buffers in the system.

A  Phosphorimetry

B  Luminometry

C  Nephelometry

D  Fluorometry

A  There would be no effect on any of the protein bands.

B  There would be an increase in the γ-globulin bands.

C  There would be an increased α1-globulin band.

D  There would be an increased β-globulin band.

A  Hydrogen redox electrode

B  Hydrogen ion-selective electrode

C  Voltammetric hydrogen electrode

D  Gas permeable PCO2 electrode

A  cholesterol using cholesterol oxidase with production of fluorescent cations.

B  urea using urease and the production of ammonium ions.

C  glucose using glucose oxidase and the production of biocarbonate ions.

D  bilirubin using bilirubin oxidase and the production of hydrogen ions.

A  has a positive charge.

B  migrates best in electrophoresis.

C  has a negative charge.

D  has no net charge.

A  is best for analytes that have a higher electrophoretic mobility.

B  involves sample injection into the capillary by applying a voltage.

C  involves sample injection into the capillary by applying a positive pressure to the sample inlet.

D  is sometimes considered to be a “biased” type of sample injection.

A  Fluorescence intensity measurements are more sensitive because the fluorophores used are very specific to the analytes they bind to and will bind to small analytes easily.

B  Absorbance measurements are more sensitive because of the ability of the monochromator to isolate very specific parts of the spectrum.

C  Fluorescence intensity measurements are more sensitive because of the use of intense light sources, signal filtering, and sensitive light emission photometers.

D  Absorbance measurements are more sensitive because the flame can break down complex compounds into elements that are specifically measured.

A  amperometry.

B  voltammetry.

C  coulometry.

D  conductometry.

A  Western blotting.

B  electrokinetic chromatography.

C  capillary electrophoresis.

D  Northern blotting.

A  Spectrophotometry and fluorescence polarization techniques

B  Fluorescence polarization and laser-induced fluorometry

C  Atomic absorption spectrophotometry and light scattering techniques

D  Laser-induced fluorometry and light scattering techniques

A  Amido Black and Coomassie Brilliant Blue

B  Coomassie Blue and ethidium bromide

C  Oil Red O and Amido Black

D  Crystal Violet and Sudan Black

A  Staining of the protein fractions will not occur if the ionic strength in the buffer is too high.

B  Increased ionic strength will lead to a backward electrophoretic pattern.

C  A heat-labile protein will become denatured if the ionic strength of the buffer is too high.

D  No migration will occur if a buffer’s ionic strength is too high.

A  nonactin

B  erythromycin

C  valinomycin

D  tetracycline

A  prism.

B  laser light.

C  hollow cathode tube.

D  tungsten light.

A  Gas permeable

B  Mercury vapor

C  Silver/silver chloride

D  Platinum