Refer to the information in the table below for questions (a) to (e): Molecular

Question

Refer to the information in the table below for questions (a) to (e): Molecular weight Number of residues Chymotrypsin (bovine pancreas Cvtochrome c (human Hemoglobin (human Lysozyme (chicken egg white) Myoglobin (equine heart Serum albumin (human Titin (human Transferrin (Drosophila A-antitrypsin (human Pepsin 25,200 12,400 64,500 14,300 16,700 66,000 2,993,000 71,800 44,300 42,100 241 104 574 129 153 609 26,926 641 418 390 9.5 10.7 6.8 11.0 7.0 4.9 6.3 6.9 5.2 (a) If you were to use size exclusion chromatography to separate the ten proteins in the table above, in what order would the proteins appear during elution from the column? Will some proteins be more difficult to separate than others? Explain why. (b) Which technique would best separate human hemoglobin and serum albumin? (c) Which technique would best separate human titin and drosophila transferrin? (d) Both cytochrome c and lysozyme have a basic pl. Which amino acids would you predict to be present in large quantities in these proteins?

Explanation / Answer

b. Hemoglobin binds to iron ions. If columns have iron ions attached to them, then by affinity chromatography method hemoglobin and serum albumin can be separated. the hemoglobin will interact with the iron affinity beads while serum albumin will be eluted out of the column.

c. Size exclusion chromatography is the best technique to separate human titin and drosophila transferrin.

d. Basic amino acids Lysine and Arginine impart positive charges to the protein. Hence, an abundance of these amino acids could be predicted in cytochrome c and lysozyme.

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