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: Excess ethanol metabolism leads to an accumulation of NADH that inhibits fatty acid metabolism.
Explanation:
Fatty acid metabolism is often activated by limited or absence of NADH, however ethanol (the main constituent of most alcoholic drinks) on metabolism yields several molecules of NADH which rather stimulates belly/abdominal fat production often referred to as "beer gut".