Essay
You have purified the receptor for a hormone by affinity chromatography.During gel filtration chromatography under native conditions the receptor elutes between pyruvate decarboxylase (250 kDa)and glutamine synthetase (620 kDa).During SDS-PAGE,in the absence of reducing agents,the receptor migrates as a single band of approximately 230 kDa.When SDS-PAGE is carried out in the presence of 2-mercaptoethanol the receptor migrates as two bands of approximately 95 and 135 kDa.Explain this result.
Correct Answer:

Verified
The receptor is a heterotetramer compose...View Answer
Unlock this answer now
Get Access to more Verified Answers free of charge
Correct Answer:
Verified
View Answer
Unlock this answer now
Get Access to more Verified Answers free of charge
Q33: The positive charge on proteins in electrospray
Q34: Proteins are synthesized in vivo by the
Q35: The salting in of proteins can be
Q36: Matching<br><br>-To help prevent denaturation of proteins in
Q37: Edman degradation can be used to<br>A)identify the
Q39: Matching<br><br>-One of the reasons the primary structure
Q40: One technique commonly used in protein purification
Q41: Which of the following amino acids would
Q42: Natural proteins most commonly contain linear polypeptides
Q43: SDS-PAGE separates proteins primarily due to differences