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.
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Answer:
The answer is A. True, salts are indeed clear because there are no free electrons to interact with ambient light.
It acts like its nothing there .
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