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Biochemistry -Protein Purification
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1. During successful purification scheme this may be expected that the
specific activity increases
specific activity decreases
number of proteins in the sample decreases
both (a) and c
2. In ion-exchange chromatography
proteins are separated on the basis of their net charge
proteins are separated on the basis of their size
proteins are separated on the basis of their shape
either (b) or c
3. Which of the following may be added to stabilize the protein after yeast cells disruption?
NaCl
Protease inhibitor
AMP
All of these
4. Gel-filtration chromatography separates on the basis of
size and shape using porous beads packed in a column
size using porous beads packed in a column
shape using porous beads packed in a column
none of the above
5. Affinity chromatography deals with the
specific binding of a protein constituents for another molecule
protein - protein interaction
protein - carbohydrate interaction
none of the above
6. 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?
1000 units/mg
10000 units/mg.
100000 units/mg
1000000 units/mg
7. Proteins separation can be carried out on the basis of
net charge
solubility in salt solutions
size or mass
all of these
8. The best way to determine the location of protein in the purification scheme is to measure the
rate of ATP synthesis
changes in the refractive index
UV absorption
mass spectroscopy of the protein
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