.
Random
Systematic
Analytical
Clinical
Ion-exchange
Partition
Affinity
Adsorption
Electrostatic Interactions
Hydrophobic Interactions
Hydrogen Bonds
Covalent Interactions
The protein has no net charge
The protein has a negative charge
The protein has a positive charge
A protein migrates best in electrophoresis
Radionnuclide used in the procedure
Substance being quantitied
Bound complex being formed in the reaction
Standard used to calibrate the method
Strength of the reaction between a multi-variant antigenic site and a single antibody combining site
Strength of the reaction between a single antigenic site and a multi-variant antibody combining site
Strength of the reaction between a single antigenic site and a single antibody combining site
Overall strength of binding between a multi-variant antigenic site and a multivalent antibody site.
Increases the solubility of macromolecules
Decreases the solubility of macromolecules
Sustains the solvation of the protein
Prevents aggregation of the protein
Proteins are amphoteric compounds
Proteins are lipid soluble
Protein charge is based on pH of the medium
Only a and b
Only a and c
By charge
By size
By molecular weight
Binding to a specific ligand
Partition
Affinity
Adsorption
Size Exclusion
Increase with increasing antigen concentration
Decrease with increasing antigen concentration
Increase with increasing antibody concentration
Decrease with increasing antibody concentration
Carboxyl and amino groups of an amino acid become unprotonated, causing the amino acid to be anionic
Carboxyl and amino groups of an amino acid become protonated, causing the amino acid to be cationic
Carboxyl group of an amino acid is dissociated and the amino group is protonated
Amino group of an amino acid is dissociated and the carboxyl group is protonated
Alkaline phosphatase
Ruthenium
Floroescein isothyocyanate
Acridium esters with H2O2
Determine the charge of a protein
Determine the molecular weight of a protein
Isolate a protein which is not denatured by process
By charge alone
By size alone
By pH and charge
By pH and size
The emission of light by a substance after absorption of excitation energy
Emission of light due to nonthermal process, a chemical reaction, or the absorption of ionizing radiation
This light is absorbed by the ground state atoms
Emission of light requiring a light source
The range of pore sizes possible is much broader
Possible to load larger quantities of material
Polyacrylamide forms gels with pores that have a much more controlled and uniform size than does agarose
All of the above
Promote destabilization of protein aggregates
Promote aggregation of hydrophobic solutes
Denature proteins
Precipitate proteins in stable structure
Alkaline Phosphatase
Ruthenium
Fluoroescein Isothyocyanate
Acridium Esters with H2O2
Decreased migration of proteins
Increased build up of heat
Decreased band resolution
Increased migration of proteins
The antibody is in excess
The antigen is in excess
Involves secondary labeled antibody
ELISA is the prototype
The proteins are separated based on their charge-to-mass ratio
SDS carries a positive charge
The proteins are separated based on their size alone
The proteins are separated based on their charge alone
A chemical reaction occurred between the buffer and all samples
The current or voltage on the power supply was set too low
Too much sample was applied to the gel
The electrophoresis chamber was not connected to a power supply
Proteins would be negatively charged and migrate towards the cathode
Proteins would be positively charged and migrate towards the anode
No migration would occur
Proteins would be postively charged and migrate towards the cathode
The strength of binding of a multivalent antigen with antibody
Strength of binding between the antibody and the multivalent antigen
Analytical sensitivity of the assay
Analytical specificity of assay
Carry the applied current
Establish charge of the solute
Both a and b
Maintain the stability of the agarose gel
All homogeneous immunoassays are one-site
All homogeneous immunoassays are competitive
All homogeneous immunoassays are fast assays
All homogeneous immunoassays are non-competitve
Current is decreased
Ionic strength of the buffer is decreased
Current is increased
Voltage is decreased
EMIT
CEDIA
ELISA
FPIA
Directly proportional to size
Inversely proportional to size
Directly proportional to rate of diffusion
By charge alone
By size alone
By size and isoelectric point
Isoelectric point alone
It is inversely proportional to electrophoretic mobility
It is directly proportional to electrophoretic mobility
It is equal to the electrophoretic mobility
There is no relationship between net charge and electrophoretic mobility
High pH
High salt concentrations
Low pH
All of the above
Decreasing concentration of Ag
At the Ag-Ab equivalence point
Increasing concentration of Ag
Decreasing concentration of Ab
Decrease with increasing antigen concentration
Increase with increasing antigen concentration
Increase with increasing antibody concentration
Decrease with increasing antibody concentration
EMIT
FPIA
ELISA
CEDIA
Of the free tracer-analyte decreases as the molecule rotates
Is directly proportional to the bound fraction of the tracer-analyte
Is increased at high concentrations of antigen
The proteins have the same charge-to-mass ratio
The proteins are separated based on their size alone
SDS carries a negative charge
The proteins are separated based on their charge
The antigen must have one epitope
The antigen must have more than one epitope
The antigen must not have an epitope
The antigen must not bind to the secondary antibody
Uses fluorochromes such as FITC
Involves the conjugation of fluorochromes to antibodies or antigens
Uses enzyme linked antibodies of antigens
Method requires use of a fluorescence detector
The antigen is in excess and the decrease in enzyme activity is directly proportional to Ag concentration
The Ab is in excess and the increase in enzyme activity is directly proportional to the Ag concentration
The Ab-Enzyme is in excess and the decrease in enzyme activity is directly proportional to the Ag concentration
The Ab-Enzyme is in excess and the increase in enzyme activity is directly proportional to Ag concentration
To distinguish between the free and bound antigens
A means in which the free antigens or Antigen-Antibody complexes can be detected
To be always in excess to increase signal to noise ratio (S/N)
All of the above
Increase
Decrease
Not be affected
Voltage x Current x Time
Voltage x Current / Time
Current x Time
Voltage x Time
Precipitate out of solution when pH of gradient is above the protein pI
Precipitate out of solution when pH of gradient is below the protein pI
Precipitate out of solution when pH of gradient is the same as the protein pI
Precipitate out of solution when fixative buffer is added
Increased migration rate of protein
Decreased migration rate of protein
No change in the rate of migration of protein
Anode
Optode
Cathode
Diode
Addition of antigen-label in excess
Addition of excess antibody
Addition of patient antigen
Addition of both patient and labeled antigens
Can be more sensitive due to the conversion of multiple substrate molecules to a multiple product molecules
Do not require antibodies
Do not require antigens
Do not require the use of an antibody-antigen reaction
A known concentration of unlabeled Ag's is added together with serum to a solid phase onto which antibodies have been bound
A known concentration of labeled Ag's is added together with serum to a solid phase onto which antibodies have been bound
An unknown concentration of unlabeled Ab's are added together with serum to a solid phase onto which antibodies have been bound
An unknown concentration of unlabeled Ab's are added together with serum to a solid phase onto which antigens have been bound
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