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Dafna1 [17]
4 years ago
12

It was found that a reversible inhibitor and a substrate bind an enzyme, but at different sites. The inhibitor was quite potent

at reducing enzyme activity, but a Scatchard analysis indicated it could not actually bind the enzyme unless the substrate was bound first. These results led to what conclusion? A. It was a competitive inhibitor. [B [U) B. It was a mixed inhibitor. C. It was an uncompetitive inhibitor. D. It was an allosteric modulator. E. It was a mechanism-based inactivator.
Chemistry
1 answer:
natita [175]4 years ago
8 0

Answer:

The correct option is C (Uncompetitive inhibitor)

Explanation:

  • Uncompetitive inhibitor takes place when an inhibitor binds at different site (allosteric site) of the enzyme after the substrate forms a complex with the enzyme.
  • The Uncompetitive inhibitors bind to a different site on the enzyme while the substrate binds to the active site on the enzyme.
  • It differs from non-competitive inhibition because non-competitive inhibition can occur with or without the presence of the substrate.
  • Uncompetitive inhibition is also referred to as Anti-competitive inhibition.
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The original concentration of the acid solution is 6.175 \times 10^-4 mol / L.

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                        HBr + NaOH -----> NaBr + H2O

There is a 1:1 equivalence with acid and base.

Moles of NaOH = 72.90 \times 10^-3 \times 0.25

                          = 0.0182 mol.

[ HBr ] = moles of base / volume of a solution

          = 0.0182 / 29.47

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A hot air balloon is filled to 1250 m3 at 27 C. At what temperature will the balloon be filled to 1600 m3 if the pressure remain
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Answer:

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Explanation:

First we convert 27 °C to K:

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With the absolute temperature we can use <em>Charles' law </em>to solve this problem. This law states that at constant pressure:

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We input the data:

300.16 K * 1600 m³ = T₂ * 1250 m³

And solve for T₂:

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