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.
Explanation:
The enzyme is unchanged so that, it can be reused when more substrate is available.
to know more ,enzymes about Biological Catalyst that are used to speed up the rate of a biological reaction but are not used up at the end of the reaction
The human body wants blood glucose (blood sugar) maintained in a very narrow range. Insulin and glucagon are the hormones which make this happen. Both insulin and glucagon are secreted from the pancreas, and thus are referred to as pancreatic endocrine hormones. The picture on the left shows the intimate relationship both insulin and glucagon have to each other. Note that the pancreas serves as the central player in this scheme. It is the production of insulin and glucagon by the pancreas which ultimately determines if a patient has diabetes, hypoglycemia, or some other sugar problem.(i hope this can help you) :)
Atoms with a covalent bond
Magma! I think and hope this helps
