Sucrosease is a tetramer of 4 identical polypeptide chains of 25 kDa. a) What wo

Question

Sucrosease is a tetramer of 4 identical polypeptide chains of 25 kDa.  

a) What would be its apparent size (mass) when analyzed by gel filtration chromatography? Why?

b) Would it elute before or after bovine serum albumin which is a monomer of 68 kDa?  Why?

c) What would be its apparent size (mass) when analyzed by SDS polyacrylamide gel electrophoresis? Why?

d) Would it migrate faster or slower than bovine serum albumin?  Why?

e) If you further knew the pI was 9.1, would it be expected to stick to an anion exchange column at pH 7.0? Why?

Explanation / Answer

a)100KDa

structure doesn't gets disrupt until unless if you add some detergent ,,,so it mass will be same

The technique can determine the quaternary structure of purified proteins that have slow exchange times, since it can be carried out under native solution conditions, preserving macromolecular interactions. SEC can also assay protein tertiary structure, as it measures the hydrodynamic volume (not molecular weight), allowing folded and unfolded versions of the same protein to be distinguished. For example, the apparent hydrodynamic radius of a typical protein domain might be 14

Related Questions

Navigate

• Browse (All)
• Browse S
• Subjects

Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.