C is the answer I would choose
It is the UPS of the cell, packing proteins from the endoplasmic reticulum, and sending it out of the cell.
Answer:
<u><em>The relationship between the</em></u><u><em> strangler fig </em></u><u><em>and the </em></u><u><em>cypress tree </em></u><u><em>closely resembles one of </em></u><u><em>parasitism</em></u><u><em> but is not. It is considered </em></u><u><em>commensalism.</em></u>
Explanation:
<em><u>Parasitism</u></em><em><u> is when one organism uses another as a host in order to survive, which generated negative impacts for the host, which will usually end in death. The strangler fig uses the tree as a host in order to sustain itself structurally but does not siphon nutrients from the tree or directly kill it, therefore it is not a form of parasitism.</u></em>
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<em><u>Commensalism </u></em><em><u>is described as a relationship between two organisms, in which the benefits are gained by only one of the members, but neither of the two is harmed in any way.</u></em>
<em><u>The relationship between the strangler fig and the cypress tree is best described as commensalism, given that although the strangler fig does eventually cause the tree to die by encircling its roots and not allowing it to grow, it does not kill the tree directly in order to survive.</u></em>
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.
Answer:
200 approximate
Explanation:
depends how many in common