1 [S] Briefly distinguish between pure noncompetitive, competitive-like, and uncompetitive like inhibition using the concepts learned during lecture. 145] 才 Identify the types of inhibition shown in each of the following scenarios where the red line indicates the effect of the inhibitor and indicate the relationship between apparent Km and Km and apparent Vmax and Vmax-

1 [S] Briefly distinguish between pure noncompetitive, competitive-like, and uncompetitive like inhibition using the concepts learned during lecture. 145] 才 Identify the types of inhibition shown in each of the following scenarios where the red line indicates the effect of the inhibitor and indicate the relationship between apparent Km and Km and apparent Vmax and Vmax-

Curren'S Math For Meds: Dosages & Sol

11th Edition

ISBN:9781305143531

Author:CURREN

Publisher:CURREN

Chapter6: Oral Medication Labels And Dosage Calculation

Section: Chapter Questions

Problem 7.2P

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For the competitive, noncompetitive and uncompetitive inhibition type investigate following figures and determine relationship between inhibitor concentration and Vmax and Km for each mechanism.
What is the minimum inhibitory concentration indicated in the following image?
Briefly describe the effects of a linear noncompetitive inhibitors on the kinetic parameters Km and Vmax. breifly discuss the reasons behind the effect of this type of inhibition on the kinetic parameters
The Michaelis-Menten rate equation for reversible mixed inhibition is written as Vo = Vmax [S] aKm + a' [S] where Vis initial velocity, Vmax is maximum velocity, [S] is substrate concentration, a represents the effect of the inhibitor bound to free enzyme (E), a' represents the effect of the inhibitor bound to the enzyme-substrate complex (ES), and Km is the Michaelis constant that represents the [S] at which the reaction reaches Vmax Vmax 2a' Apparent, or observed, Km is equivalent to the [S] at which Vo = Derive an expression for the effect of a reversible inhibitor on apparent Km from the previous equation. Use the alphabet tab to enter a and the basic tab to enter the prime sign in your answer. apparent Km =
Identify the two forms of mixed inhibition and briefly describe how the two forms differ?
1. Inhibitor Impact Factor Practice calculations with the inhibitor impact factor (IIF).(a) For Ki = 2 μM and [I] = 0.1 μM, what is IIF?(b) For Ki = 2 μM and [I] = 10 μM, what is IIF?(c) Calculate impact on KM-app and Vmax-app for a competitive inhibitor for the conditiondescribed in (a) and as described in part (b).(d) Calculate impact on KM-app and Vmax-app for a non-competitive inhibitor for the conditiondescribed in (a) and as described in part (b).(e) Briefly explain in terms of molecules why the condition described in (a) has a negligibleimpact on enzyme performance AND why the condition described in (b) has a much largerimpact on enzyme performance. Pictures and words.
Why does the apparent KM decrease in the presence ofan uncompetitive inhibitor?
The Michaelis-Menten rate equation for reversible mixed inhibition is written as Vo = Vmax [S] aKm + a' [S] where Vo is initial velocity, Vmax is maximum velocity, [S] is substrate concentration, a represents the effect of the inhibitor bound to free enzyme (E), a' represents the effect of the inhibitor bound to the enzyme-substrate complex (ES), and Km is the Michaelis constant that represents the [S] at which the reaction reaches/Vm Vmax 2α' Derive an expression for the effect of a reversible inhibitor on apparent Km from the previous equation. Use the alphabet tab to enter a and the basic tab to enter the prime sign in your answer. = Apparent, or observed, Km is equivalent to the [S] at which Vo max. apparent Km =
The Michaelis-Menten rate equation for reversible mixed inhibition is written as Vo Vmax [S] aKm + a' [S] where Vo is initial velocity, Vmax is maximum velocity, [S] is substrate concentration, a represents the effect of the inhibitor bound to free enzyme (E), a' represents the effect of the inhibitor bound to the enzyme-substrate complex (ES), and Km is the Michaelis constant that represents the [S] at which the reaction reaches Vmax Apparent, or observed, K is equivalent to the [S] at which Vo max Derive an expression for the effect of a reversible inhibitor on apparent K from the previous equation. Use the alphabet tab to enter a and the basic tab to enter the prime sign in your answer. apparent Km =
A. Lineweaver-Burk plot of the enzyme with increasing amounts of substrate in the absence or the presence of the inhibitor is shown below. Graph A : x-intercept Graph B : x-intercept = - 0.012, y-intercept = 0.8 Graph C : x-intercept = - 0.027, y-intercept = 0.8 Graph D : x-intercept = - 0.039, y-intercept = 0.8 - 0.007, y-intercept = 0.8 Graph A 4 Graph B Graph C Graph D 1 -0,04 -0,02 0,00 0,02 0,04 1/[Substrate] (uM) (i) Which graph indicates an enzymatic reaction without inhibitor? (ii) Which type of inhibitor is it? Briefly explain. (iii) Which graph indicates the highest concentration of inhibitor? (iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers. 1/Rate (umol/min)
Find the control Vmax and Km value, and use this to find the Vmax apparent for inhibitor A.
Given a graph for uncompetitive inhibition, where could we obtain a number that could be used to calculate: a) Km b) Vmax (Need to know an exact location on the graph, but I don't understand how to go about this)