A. Which one of the following is an example of affinity chromatography? Select all that apply. a) Hormone – receptor interaction d) All of the above b) Enzyme - substrate interaction c) Antigen-antibody interaction e) Cytochrome C – DEAE matrix

Biochemistry
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Chapter1: Biochemistry: An Evolving Science
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A. Which one of the following is an example of affinity chromatography? Select all that apply.
a) Hormone – receptor interaction
b) Enzyme – substrate interaction
c) Antigen-antibody interaction
d) All of the above
e) Cytochrome C – DEAE matrix
B. If your sepharose beads are covalently attached to adrenaline hormone, which of the following
protein is most likely purified by affinity chromatography?
a) Receptor tyrosine kinase (RTK)
b) Calmodulin
c) GPCR
d) Protein kinase A
C. Which of the following malate dehydrogenase (MDH) has a 'peptide epitope tag'?
a) MDH-HA
b) MDH-GST
c) MDH-GFP
e) All of them
D. To elute target proteins from an affinity chromatography matrix, which of the following
conditions would be the most appropriate?
a) Low salt concentrations
b) High salt concentrations
c) Adding a soluble ligand that competes with the affinity tagged protein for binding to the column
d) Just keep washing buffer through the column, isocratic elution
Transcribed Image Text:A. Which one of the following is an example of affinity chromatography? Select all that apply. a) Hormone – receptor interaction b) Enzyme – substrate interaction c) Antigen-antibody interaction d) All of the above e) Cytochrome C – DEAE matrix B. If your sepharose beads are covalently attached to adrenaline hormone, which of the following protein is most likely purified by affinity chromatography? a) Receptor tyrosine kinase (RTK) b) Calmodulin c) GPCR d) Protein kinase A C. Which of the following malate dehydrogenase (MDH) has a 'peptide epitope tag'? a) MDH-HA b) MDH-GST c) MDH-GFP e) All of them D. To elute target proteins from an affinity chromatography matrix, which of the following conditions would be the most appropriate? a) Low salt concentrations b) High salt concentrations c) Adding a soluble ligand that competes with the affinity tagged protein for binding to the column d) Just keep washing buffer through the column, isocratic elution
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