Answer:
More than one of the above
Explanation:
I strongly recommend sticking with the prescribed dosage of a drug.
A drug works by binding itself to the receptor site of a cell or tissue by non-covalent interactions.
Repeated doses of the same drug however may make the drug start behaving as an inverse agonist by blocking (instead of binding) the receptor site of the cell thus inducing a reduced response instead of an increased response to the drug.
Answer:
These microbes conduct photosynthesis: using sunshine, water and carbon dioxide to produce carbohydrates and, yes, oxygen. In fact, all the plants on Earth incorporate symbiotic cyanobacteria. For some untold eons prior to the evolution of these cyanobacteria, during the Archean eon, more primitive microbes lived the real old-fashioned way: anaerobically. These ancient organisms—and their "extremophile" descendants today—thrived in the absence of oxygen, relying on sulfate for their energy needs. But roughly 2.45 billion years ago, the isotopic ratio of sulfur transformed, indicating that for the first time oxygen was becoming a significant component of Earth's atmosphere,
Answer:
Roundworm
Explanation:
Unsegmented kicks out the possibility of A or D. Roundworms are pointed at their ends and have distinct males and females
Is c a and b i hope im right
Answer:
The correct answer is option c. "The apparent value of KM increases with a competitive inhibitor, while it remains unchanged with a noncompetitive inhibitor".
Explanation:
The KM value in an enzymatic reaction is defined as the substrate concentration at which the half of the enzyme molecules are binding with the substrate. A way to distinguish between a competitive and noncompetitive inhibition is that the apparent value of KM increases with a competitive inhibitor, while it remains unchanged with a noncompetitive inhibitor. A competitive inhibitor would make that a higher concentration of substrate is needed, while a noncompetitive inhibitor does not change KM since the inhibitor binds to a site of the enzyme different from the active site.
