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Different types of chromatography exploit different protein differences
Size (molecular weight)
Gel filtration
Isoelectric point
Ion-exchange
Solubility
Hydrophobic interaction
Ion-exchange
Based on charge interaction
Ion-exchanger column = positively charged
E.g/ diethylaminoethyl
How proteins are detected in ion-exchange
Use easily detectable proteins
Methaemolglobin - absorbs light at 410nm
Green fluorescent protein - absorbs at 490nm
MetHb passes through low ionic strength buffer - pH = 7.2
GFP binds to DEAE cellulose - pH 5.8
Elute GFP with high ionic strength infer
Percentage yield
(total amount of protein recovered from the column)/(total amount of proteins applied to the column)