Protein Purification

Question: Affinity chromatography deals with the
[A].

specific binding of a protein constituents for another molecule

[B].

protein – protein interaction

[C].

protein – carbohydrate interaction

[D].

none of the above

Answer: Option A

Explanation:

No answer description available for this question.

Question: In ion-exchange chromatography
[A].

proteins are separated on the basis of their net charge

[B].

proteins are separated on the basis of their size

[C].

proteins are separated on the basis of their shape

[D].

either (b) or (c)

Answer: Option A

Explanation:

No answer description available for this question.

Question: Gel-filtration chromatography separates on the basis of
[A].

size and shape using porous beads packed in a column

[B].

size using porous beads packed in a column

[C].

shape using porous beads packed in a column

[D].

none of the above

Answer: Option A

Explanation:

No answer description available for this question.

Question: During successful purification scheme, this may be expected that the
[A].

specific activity increases

[B].

specific activity decreases

[C].

number of proteins in the sample decreases

[D].

both (a) and (c)

Answer: Option D

Explanation:

No answer description available for this question.

Question: A purified protein sample contains 10 μg of protein and has an enzyme activity of 1 m mole of ATP synthesized/sec (1 unit). What is the specific activity of the final purified sample?
[A].

1,000 units/mg

[B].

10,000 units/mg.

[C].

100,000 units/mg

[D].

1,000,000 units/mg

Answer: Option C

Explanation:

No answer description available for this question.

Question: The best way to determine the location of protein in the purification scheme is to measure the
[A].

rate of ATP synthesis

[B].

changes in the refractive index

[C].

UV absorption

[D].

mass spectroscopy of the protein

Answer: Option A

Explanation:

No answer description available for this question.