Answer:
This protein consists of 8 subunits of equal size linked by disulfide bonds
Explanation:
The sodium dodecyl sulfate-polyacrylamide gel (SDS-PAGE) is a technique widely used in molecular biology laboratories to separate proteins with molecular weights between 5 and 250 kDa. SDS is an anionic detergent used to denature proteins before electrophoresis. SDS can denature proteins by altering non-covalent bonds such as hydrogen, hydrophobic and ionic interactions, but they cannot cleave disulfide bonds. In this case, reducing agents (e.g., β-mercaptoethanol or dithiothreitol) have been used to cleave disulfide bonds.
Answer:
voluntary, you did it by will
Explanation:
I did not quite understand that but in pretty sure it is b
<span>Tariffs shield new industries in the early stages of their development from the competition of more mature rivals.</span>
