2 a. You are trying to purify protein C from a mixture of proteins noted in the above Table. If you had only one type of column to choose from, which one would allow you to purify protein C with the least number of contaminants? Size exclusion column Ion exchange column Affinity chromatography using glucose as the bait Affinity chromatography using NAD as the bait   Please explain why you chose the column above based upon the properties of the column AND the proteins in the Table.

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ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter18: Glycolysis
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2 a. You are trying to purify protein C from a mixture of proteins noted in the above Table. If you had only one type of column to choose from, which one would allow you to purify protein C with the least number of contaminants?

Size exclusion column
Ion exchange column
Affinity chromatography using glucose as the bait
Affinity chromatography using NAD as the bait
 
Please explain why you chose the column above based upon the properties of the column AND the proteins in the Table.
CH2
H2C
HO
H2
_0
H.
+
CH
H2C.
Enzyme X is an aspartyl protease. Here is the tetrahedral intermediate in the active site of
Enzyme X. What is the amino acid sequence of the two products of the reaction?
Product 1
Enter your answer here
Product 2
Enter your answer here
ZI
Transcribed Image Text:CH2 H2C HO H2 _0 H. + CH H2C. Enzyme X is an aspartyl protease. Here is the tetrahedral intermediate in the active site of Enzyme X. What is the amino acid sequence of the two products of the reaction? Product 1 Enter your answer here Product 2 Enter your answer here ZI
Protein
Molecular
Isoelectric
Ligand
point (pl)
weight
(kDa)
A
40
7
glucose
В
20
NAD
glucose
glucose
glucose
400
7
35
8.
E
10
6.
Transcribed Image Text:Protein Molecular Isoelectric Ligand point (pl) weight (kDa) A 40 7 glucose В 20 NAD glucose glucose glucose 400 7 35 8. E 10 6.
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