Answer:
This signifies that the protein primarily comprises multiple polypeptide chains connected together with the help of disulfide bonds. The enzymes may be found in the form of dimers, trimers, or tetramers. Various examples of dimers, trimers, and tetramer proteins are known, of them, NEMOs dimers are considered to be held by disulfide bonds.
Thus, it can be hypothesized that the enzyme under examination is a multimer held in combination by disulfide bonds, with each comprising catalytic sites. On breaking of disulfide bonds, the enzyme dissociates into its many single units.
This illustrates the reduction in catalytic activity. Each active site in a single unit will work, however, at a gradual rate. This also shows detection of multiple globular proteins after disulfide reduction.
Central government.state government control
Answer:
It decreases the levels of cAMP in the cell, repressing transcription from the lac operon.
Explanation:
When glucose is absent, cAMP serves as coactivator binds to CRP, the catabolite gene activator protein. The CRP-cAMP complex binds to the site near the lac promoter and stimulates the expression of the operon by RNA polymerase many folds.
Catabolite repression refers to inhibition of the synthesis of enzymes of lactose catabolism when glucose is present as an energy source. In the presence of glucose, synthesis of cAMP is inhibited resulting in its lower cellular concentration. The lower cAMP levels do not allow the binding of cAMP and CRP. The result is reduced expressed of lac operon.
The rapid release of air/ gas bubbles during cooling
B! The strongest characteristics will survive when the weak ones won't
