Learning Materials
Features
Discover
Chapter 12: Q9. (page 398)
At what concentration of (expressed as a multiple of ) will ?
The concentration of at which is.
Over 30 million students worldwide already upgrade their learning with Vaia!
All the tools & learning materials you need for study success - in one app.
Get started for free
Based on some preliminary measurements, you suspect that a sample of enzyme contains an irreversible enzyme inhibitor. You decide to dilute the sample 100-fold and remeasure the enzyme's activity. What would your results show if an irreversible inhibitor is present?
If there is 10 μmol of the radioactive isotope ³²P (half-life 14 days) at t=0, how much will ³²P remain at (a) 7 days, (b) 14 days, (c) 21 days,
and (d) 70 days?
Ethanol in the body is oxidized to acetaldehyde (CH₃CHO) by liveralcohol dehydrogenase (LADH). Other alcohols are also oxidized byLADH. For example, methanol CH₃OH), which is mildly intoxicating, isoxidized by LADH to the quite toxic product formaldehyde (CH₂O). Thetoxic effects of ingesting methanol (a component of many commercialsolvents) can be reduced by administering ethanol. The ethanol acts as acompetitive inhibitor of the methanol by displacing it from LADH. Thisprovides sufficient time for the methanol to be harmlessly excreted bythe kidneys. If an individual has ingested 100 mL of methanol (a lethaldose), how much 100 proof whiskey (50% ethanol by volume) must beimbibe to reduce the activity of his LADH toward methanol to 5% of itsoriginal value? The adult human body contains -40 L of aqueous fluidsthroughout which ingested alcohols are rapidly and uniformly mixed.The densities of ethanol and methanol are both 0.79 g .cm-3. Assumethe KM values of LADH for ethanol and methanol to be 1.0 X 10⁻³Mand 1.0 X 10⁻²M, respectively, and that KI = KM for ethanol.
For an enzyme-catalyzed reaction, the presence of 5 nM of a reversible inhibitor yields a Vmax value that is 80% of the value in the absenceof the inhibitor. The KM value is unchanged. (a) What type of inhibition is likely occurring? (b) What proportion of the enzyme molecules have bound inhibitor? (c) Calculate the inhibition constant.
You are constructing a velocity versus [substrate] curve for an enzyme whose KM is believed to be about 2 μM. The enzyme concentration is 200 nM and the substrate concentrations range from 0.1 μM to 10 μM. What is wrong with this experimental setup and how could you fix it?
What do you think about this solution?
We value your feedback to improve our textbook solutions.
Explanations 
Textbooks 
Exams 
GCSE 
IGCSE 
AS 
A Level 
International A Level 
University Admissions Tests 
Flashcards 
Vaia AI 
Notes 
Study Plans 
Study Sets 
Find a job 
Find a degree 
Student Deals 
Magazine 
Mobile App