What reagents can be used to break disulfide bonds?
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Answer / raghavendra naidu
1)DTT- Di thio tritol
2)BME- Beta mercapto ethanol
| Is This Answer Correct ? | 38 Yes | 0 No |
Answer / g.rajesh kumar
Mercaptoethanol breaks the disulphide bonds in proteins and
sds makes the protein to possess negative charge, so that
proteins can be separated based on their charge in sds-page
chromatography.
| Is This Answer Correct ? | 23 Yes | 1 No |
Answer / narayana
Di thio thretol,Beta marcapto ethanol.
Some times urine also.
| Is This Answer Correct ? | 2 Yes | 0 No |
Answer / g satheesh
sodium bisulfite in Base media or Zinc and acetic acid
| Is This Answer Correct ? | 3 Yes | 2 No |
Answer / kesava.sat@gmail.com
SDS pocess the proteins to positive charge and b-mercato ethanol degrades the disulphide bonds. and urea also degrades the disulphide bonds
| Is This Answer Correct ? | 1 Yes | 4 No |
What factors cause salting in and salting out of macromolecules?
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Many genes are regulated in both a negative and a positive manner. The genes mediating lactose metabolism in bacteria are a classical example. What are the two small molecule ligands that control expression of these genes? What does each one do?
1 Answers Pace Pharmaceuticals,
What is the phenomenon of salting-in effect?
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