Module 2 Quiz

A  4.68 g/dL

B  Albumin values cannot be calculated using densitometry.

C  0.065 g/dL

D  15.4 g/dL

A  Conductivity-based measurement

B  Amperometric method

C  Ion-selective electrode

D  Coulometric method

A  a shorter wavelength.

B  a higher energy.

C  the same wavelength.

D  a lower energy.

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

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

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

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

A  more efficient heat dissipation for better separation.

B  the small sample size required.

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

D  the increased amount of time required for separation.

A  Fluorometry

B  Nephelometry

C  Phosphorimetry

D  Luminometry

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 β-globulin band.

D  There would be an increased α1-globulin band.

A  Voltammetric hydrogen electrode

B  Hydrogen ion-selective electrode

C  Gas permeable PCO2 electrode

D  Hydrogen redox electrode

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

B  cholesterol using cholesterol oxidase with production of fluorescent cations.

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

D  urea using urease and the production of ammonium ions.

A  migrates best in electrophoresis.

B  has no net charge.

C  has a negative charge.

D  has a positive charge.

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

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

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

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

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

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

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

D  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.

A  amperometry.

B  coulometry.

C  conductometry.

D  voltammetry.

A  Northern blotting.

B  electrokinetic chromatography.

C  Western blotting.

D  capillary electrophoresis.

A  Fluorescence polarization and laser-induced fluorometry

B  Atomic absorption spectrophotometry and light scattering techniques

C  Spectrophotometry and fluorescence polarization techniques

D  Laser-induced fluorometry and light scattering techniques

A  Amido Black and Coomassie Brilliant Blue

B  Coomassie Blue and ethidium bromide

C  Crystal Violet and Sudan Black

D  Oil Red O and Amido Black

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

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

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

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

A  valinomycin

B  tetracycline

C  nonactin

D  erythromycin

A  prism.

B  hollow cathode tube.

C  laser light.

D  tungsten light.

A  Platinum

B  Silver/silver chloride

C  Gas permeable

D  Mercury vapor