Final answer:
To separate the peptides produced by chymotrypsin treatment, electrophoresis and size exclusion chromatography would be effective methods. Additionally, chromatography on either a cationic or an anionic column could be used, depending on the peptides' charge properties at the given pH.
Step-by-step explanation:
The peptides produced by chymotrypsin treatment can be separated using several methods:
- Electrophoresis: This technique separates peptides based on their charge under an electric field. Peptides move at different rates depending on their charges, allowing for their separation.
- Chromatography: There are several types of chromatography that can be utilized:
- Chromatography on a cationic column at pH=7: This method would separate peptides based on their interaction with positively charged particles in the column.
- Size exclusion chromatography: This technique separates peptides based on their size, as smaller peptides will pass through the pores of the column more easily than larger ones.
- Chromatography on an anionic column at pH=4: Peptides would be separated based on their interaction with negatively charged particles in the column.
Considering the properties of the peptides, suitable methods for their separation would include electrophoresis, size exclusion chromatography, and depending on the charge properties of the peptides, either cationic or anionic chromatography at the appropriate pH.