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.
Phospholipid can occur in a polar cell.
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Find latitude and longitude
<span>A river delta forms by the deposition of sediments from the river when it slows to join a larger body of water.</span>
Answer:
B-Close the ring in the bearing or the ring in the bearing.
Explanation:
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