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13 Cards in this Set
- Front
- Back
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Absorption stage of ion chromatography |
The compounds to be separated are loaded at the top of the column, and are “washed” down with the mobile phase (the buffer). |
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Elution or deabsorption stage |
Remove bound compounds back into the mobile phase,and by that accomplish additional separation |
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How is elution accomplished |
by adding increasing concentrations of salt ions in the mobile phase.These ions compete with the amino acids for binding the resin and at high enough forcing them all out |
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When do amino acids not bind (chromatography) |
At a pH above the pI of an amino-acid,it will be negatively charged and will not bind to an Cation exchanger |
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Sixe exclusion chromatography also known as |
‘Gel filtration’ and ‘Molecular sieving |
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Size exclusion separates based on |
MW or ‘Stokes radius ’ |
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Method of affinity chromatography |
Separates proteins based on biological function |
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Polymer used in gel electrophoresis |
Acrylamide |
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What are proteins mixed with in gel electrophoresis |
Sodium docecly sulfate (anion detergent) and beta mercaptoethanol (denaturing agent) |
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What does beta mercaptoethanol do |
Disrupts secondary, tertiary amd quatenary structure to give a linear peptide |
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How does SDS bind |
Stoichiometrically |
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3 important things with SDS page |
SDS provides uniform charge, native protein shape is irrelevant, rate of movement depends on size |
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Isoelectric focusing |
Allows for separation of proteins in a gel based on their relative amounts of acidic and basic amino acids |
