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Zigmanuir [339]
3 years ago
11

The benefit of measuring the initial rate of a reaction, V0, is that early in the course of the reaction, A) Km is the substrate

concentration at which V0 = Vmax. B) The rate of product formation is linear and [S] has not been lowered significantly. C) V0 is least responsive to changes in [S]. Km will be lower, so the enzyme will bind S better. D) V0 will be independent of enzyme concentration.
Biology
1 answer:
aleksandr82 [10.1K]3 years ago
4 0

Answer:

Rate of product formation is linear and [S] has not been lowered significantly.

Explanation:

The rate of enzyme-catalyzed reactions is affected by several factors, the contraction of substrates [S] is one of them. The substrate concentration keeps on changing as the reaction proceeds. This is why the reaction rate is measured at the initial stages of reactions when the substrate concentration [S] is much greater than the concentration of the enzyme. It is called the initial rate or initial velocity.

Under the conditions of higher substrate concentration and relatively much lower enzyme concentrations, only a few molecules of substrates are being converted into product. At a relatively higher substrate concentration, the rate of product formation increases linearly.

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3 0
2 years ago
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sladkih [1.3K]

Answer:

Explanation:

Enzymes are biological catalysts; catalysts are substances that increase the rate of chemical reactions without being used up (BBC, 2010), without these catalysts it would take an extremely long time for these reactions to take place. The enzyme used in this particular experiment was pepsin; pepsin is a zymogen of pepsinogen. Pepsinogen is activated by hydrochloric acid, which is released from parietal cells in the stomach lining. The hormone gastrin and the vagus nerve trigger the release of both pepsinogen and hydrochloric acid from the stomach lining when food is ingested. Hydrochloric acid creates an acidic environment, which allows pepsinogen to unfold and cleave itself in an autocatalytic fashion, generating pepsin. (Life Science Network, 2010)

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