How does ion-exchange chromatography separate proteins?
Answer: It separates proteins on the basis of their charge when anions or cations bind negatively or positively charged groups. For example, when salt cations (like NaCl) are being exchanged, negatively charged proteins will pass through, while positively charged proteins will stick.
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Bio Chemistry
- What is an international unit (IU) in enzyme kinetics?
- What is the slope in the Lineweaver-Burk plot?
- How do you overcome competitive inhibition?
- What does the turnover number mean in enzyme kinetics?
- What happens during uncompetitive inhibition?
- What happens during noncompetitive inhibition?
- What happens during competitive inhibition?
- What are the non-covalent modes of inhibition?
- Why is the Induced Fit Model deemed to be more correct than the Lock and Key Model?
- What are the two models of substrates binding to enzymes, and which is deemed to be more correct?
- What are the definitions of apoenzymes and holoenzymes and what is the difference between them?
- What are the definitions of apoproteins and holoproteins and what is the difference between them?
- True or false: All cofactors are coenzymes.
- Pertaining to enzymes, what is a cofactor?
- What does the fourth number indicate in the Enzyme Commission number for an enzyme?
- What does the third number mean in the Enzyme Commission number of an enzyme? (hint: it is directly related to the second number)
- What does the second number mean in the Enzyme Commission number of an enzyme?
- In the four-letter coding (Enzyme Commission number) of enzymes, what does the first digit signify?
- What are the six classes of enzymes, and what are their numbers according to the enzyme commission numbering system?
- How exactly do active sites catalyze reactions when a substrate is bound to it?
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- How does mass spectrometry (electrospray ionization) separate proteins?
- How does electrophoresis separate proteins?
- How does gel-filtration separate proteins?