Determine the Ki for the inhibitor at 30 °Cand decidewhat type of inhibitor is being used.EoTISV(g/I)(°C)(mmol/ml)(mmol/ml)(mmol/ml-min)1.6300.12.631.6300.0331.921.6300.021.471.6300.010.961.6300.0050.561.649.60.15.131.649.60.0333.701.649.60.011.891.649.60.00671.431.649.60.0051.110.92300.11.640.92300.020.900.92300.010.580.92300.60.11.330.92300.60.0330.800.92300.60.020.57

Answered: Determine the Ki for the inhibitor at…

Science

Biochemistry

Determine the Ki for the inhibitor at 30 °Cand decide what type of inhibitor is being used.

Curren'S Math For Meds: Dosages & Sol

11th Edition

ISBN:9781305143531

Author:CURREN

Publisher:CURREN

Chapter10: Reconstitution Of Powdered Drugs

Section: Chapter Questions

Problem 9SST

See similar textbooks

Related questions

Q: Suggest a simple method to determine whether a reaction is being inhibited by a competitive or…

A: Inhibitorsis a substance that reduces or decreases the activity of an enzyme. It inhibits the proper…

Q: Kcat/Km is an indicator of: Select one: O a. catalytic power. O b. catalytic efficiency. O c.…

A: The active sites of an enzyme are typically made up of amino acid residues; the specificity of the…

Q: a compettitive inhibitor interferes with?

A: The enzyme generally binds with the substrate but in competitive inhibition, the inhibitor is…

Q: In this setup, the rate of the reaction can be increased by

A: Photosynthesis is the process by which plants synthesize their own food in the presence of sunlight.…

Q: describe the mechanism of each class of inhibitor, including how they impact the effective…

A: There are mainly four types of inhibitors . Competitive inhibitor Non-competitive inhibitor…

Q: what is the relative activity and the degree of inhibition caused by a competitive inhibitor when…

A: Enzymes are catalysts that enhance the rates of biochemical reactions (biological catalysts).…

Q: For the competitive, noncompetitive and uncompetitive inhibition type investigate following figures…

A: The enzyme inhibition is the regulatory mechanism of the enzyme. They are of two types, irreversible…

Q: In the estimation of glucose with benedict's reagent, what is resposnible for the white precipitate…

Q: Compare (linear) competitive inhibition with mixed inhibition, by referring to the similarities and…

A: solution In case of mechanism : 1) In competitive inhibition, binding of an inhibitor prevents…

Q: Define the term minimum inhibitory concentration and their uses.

A: Minimum inhibitory concentration (MIC) is the term used by microbiologists to test the minimum drug…

Q: True or False. If drug A produces a larger zone of inhibition than drug B on the Kirby-Bauer disk…

A: Introduction If drug A does produce a larger zone of inhibition, that is one positive attribute of…

Q: H. Draw a plot showing reaction velocity as a function of substrate concentration for Ks = 50 µM,…

A: As here given in the question, Vmax= 5uM S-1 Ks=50uM and Ki = 250uM both in presence and absence of…

Q: 78. Which situation(s) might result in a higher than expected plasma drug concentration? a. Enzyme…

A: The volume of distribution (vd) of a drug describes the total amount of a drug and the plasma…

Q: List the criteria used to select a buffer for a biochemical reaction.

A: A Buffer resist change in pH when acid or base is added. There are two types of buffer: Mixture of…

Q: Determine the extent of advantage in terms of G factor reduction if a kraft cooking temperature is…

A: Diffusion is the process in which the gaseous molecules spread out and occupy the volume of the…

Q: How can you distinguish between a competitive inhibitor and an uncompetitive inhibitor…

A: Competitive inhibitor- In competitive inhibitor, an inhibitor that resembles the normal substrate…

Q: Use the plot provided to estimate Km and Vmax values for both with and without inhibitor of the…

A: Those proteins which help to speed up the chemical reaction are referred to as enzymes. The rate of…

Q: I have the substrate concentration as 20, 40 , 65 and the V(mol/min) no inhibitor 602, 690, 833 and…

A: MM plot is Michaelis menton plot that is constructed with Substrate concentration on x axis and Vo…

Q: From the active site diagram below, please indicate the cofactor from the indicated components. HO 4…

A: Cofactors are the non protein molecules that help the enzyme to carry out catalysis. Enzymes without…

Q: Determine Km and Vmax using Lineweaver-Burke in the presence and absence of inhibitor. What type of…

A: Michaelis menten constant, Km is the substrate concentration required to produce half maximum…

Q: Describe Bohr effect and give its physiological significance

A: Hemoglobin is present in the RBCs of humans and acts as a carrier for the oxygen gas in living…

Q: Identify the two forms of mixed inhibition and briefly describe how the two forms differ?

A: The substance that inhibit the activity of enzymes are called enzyme inhibitors and the mechanism by…

Q: what is the relative activity and the degree of inhibition caused by a competitive inhibitor when…

A: Enzymes are biocatalyst that increases the speed of reaction by lowering the activation energy.…

Q: Calculate the ratio of [fumarate] to [succinate] under cellular conditions at 37°C.

A: Fumarate and succinate are the intermediate products or metabolites of the citric acid cycle. By the…

Q: Classify the enzyme inhibitors by giving the names, mechanisms, and effect on the kinetic parameters…

A: Enzymes are bio-catalyst. They increase the speed of reaction by lowering its activation energy.…

Q: Given the active site diagram below, identify the mechanism(s) of catalysis. 5 2 Metal ion Induced…

A: active site is a region on an enzyme that binds to a protein or other substance during a reaction.

Q: Determine whether or not reaction is a redox reaction. For each redox reaction, identify the…

A: Redox reaction is considered as a process, during which one element is must be reduced or oxidized…

Q: Given the active site diagram below, identify the mechanism(s) of catalysis. 2 1 5 Metal ion Induced…

A: Acid-base catalysis, metal ion catalysis, approximation etc are some of the mechanisms through…

Q: Which statement is consistent with these data? Compound X is an allosteric activator and Compound Z…

A: Enzyme catalyzed reaction is the conversion of substrate molecules into product molecules in…

Q: Briefly explain the role of the oxyanion hole for the catalysis of chymotrypsin.

A: Chymotrypsin is a seine protease. Serine protease is a class of enzyme in which catalytic mechanism…

Q: 460 410 360 310 260 210 160 110 60 -10 -S10 5 10 15 20 25 30 35 40 45 50 55 1/IS] per mM 1. What…

A: Enzymes are biocatalyst that are responsible for performing specific reaction within the body. They…

Q: Describe non-competitive inhibition.

A: Enzymes are protein that increases the rate of reaction by lowering the activation energy. Enzymes…

Q: Calculate the Km of the enzyme with these parameters. kcat = 130s^-1 Vo = 3.0 μMs-1 S = 10 μM…

A: Km of an enzyme is known as Michalis constant, which denotes the substrate concentration at which…

Q: Give two advantages and two disadvantages to using the biuret reaction to measure protein…

A: Aromatic amino acids such as tyrosine, tryptophan and phenylalanine exhibit strong UV-light…

Q: How would a competitive inhibitor change the Km and the Vmax for an enzyme? Explain why a…

A: A competitive inhibitor is interruption of a chemical pathway owing to one chemical substance…

Q: The following data were obtained in the presence and absence of inhibitor. Rate without Rate with…

A: Enzyme inhibition refers to the decrease in enzyme related processes, enzyme production, and enzyme…

Q: Write the difference between compititive and non compititive enzyme inhibitors.

A: Enzyme inhibitors binds with the active sites of enzymes and reduces the compatibility of substrate…

Q: For which purpose the method of measuring biochemical demand is used?

A: Most natural waters contain small quantities of organic compounds. Aquatic microorganisms have…

Q: Calculate KI' of the inhibitor from the information given. All information may not be needed to…

A: Enzyme inhibition refers to the decrease in enzyme related processes which may be enzyme production…

Q: Calculate the specific activity and kcat for this enzyme

A: Enzymes are catalyst that speed up the biochemical reaction by lowering the activation energy of the…

Q: Explain why structure 4 is a more potent inhibitor (lower IC50 value) than inhibitor 3 and why…

A: IC50 is the total concentration of inhibitor that is required to reach 50% inhibition. This means…

Q: make a flow chart of a drug and show its metabolism noting if there are active metabolites where…

A: Drug metabolism occurs primarily in liver. Although drug is inactivated by metabolism, some drug…

Q: What role does SDS, isopropanol, 70% ethanol, lysis solution and precipitating solution play and…

A: DNA extraction is a procedure used to isolate DNA from the nucleus of cells. When an ice-cold…

Q: Given the active site diagram below, indicate the mechanism(s) of catalysis. 5 HO OH HN OH *HN NH…

A: The figure in question shows the mechanism of formation of transition state. By analyzing the active…

Concept explainers

Metabolic pathways

Metabolism is defined as the group of life-supporting, enzyme-mediated chemical reactions in organisms. A metabolic pathway is a set of these chemical reactions that involve anabolism (synthesis of complex biomolecules) and catabolism (breakdown of biomolecules into small molecules) that occur inside a cell. Metabolites are the reacting substances, products, and intermediate substances of an enzymatic process that are altered by a series of chemical events catalyzed by enzymes.

Question

Determine the Ki for the inhibitor at 30 °Cand decide
what type of inhibitor is being used.
Eo
T
I
S
V
(g/I)
(°C)
(mmol/ml)
(mmol/ml)
(mmol/ml-min)
1.6
30
0.1
2.63
1.6
30
0.033
1.92
1.6
30
0.02
1.47
1.6
30
0.01
0.96
1.6
30
0.005
0.56
1.6
49.6
0.1
5.13
1.6
49.6
0.033
3.70
1.6
49.6
0.01
1.89
1.6
49.6
0.0067
1.43
1.6
49.6
0.005
1.11
0.92
30
0.1
1.64
0.92
30
0.02
0.90
0.92
30
0.01
0.58
0.92
30
0.6
0.1
1.33
0.92
30
0.6
0.033
0.80
0.92
30
0.6
0.02
0.57

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

SEE SOLUTION Check out a sample Q&A here

Step 1

VIEW

Step 2

VIEW

Step by step

Solved in 2 steps with 2 images

SEE SOLUTION Check out a sample Q&A here

Knowledge Booster

Learn more about

Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.

Similar questions

Define the term minimum inhibitory concentration and their uses.
What are the: a.)Active Ingredient Classification (ex. Analgesic) B.) Brand Names available in the market(ex. Biogesic) C.) Label claim (ex. 500 mg/tablet, 160 mg/5 mL).d.) Dosage forms available in the market (ex. tablet) and matter classification (ex. solid/liquid/gas – homogeneous/ heterogeneous E.)Dosage and regimen (ex. take #1 500 mg tablet every 4 hours) f.)Pharmacologic Use or Indication. of a precipitated sulfur or the one at the third row only?
Using conversion factors, solve each of the following clinical problems:a. The physician has ordered 1.0 g of tetracycline to be given every six hours to a patient. If your stock on hand is 500-mg tablets, how many will you need for one day’s treatment?b. An intramuscular medication is given at 5.00 mg / kg of body weight. What is the dose for a 180-lb patient?c. A physician has ordered 0.50 mg of atropine, intramuscularly. If atropine were available as 0.10 mg /mL of solution, how many milliliters would you need to give?d. During surgery, a patient receives 5.0 pt of plasma. How many milliliters of plasma were given?
Discuss the biochemical effects of acute vs. chronic ethanol intoxication and show thesignificant differences between these two states on patient management.
Why does a pure noncompetitive inhibitor not changethe observed KM?
Using the provided data on the activity part, what is the acquired R value? Is it acceptable or not? If not, what laboratory techniques should be improved? Concentration Absorbance 6 3.69267 8 3.69667 10 3.69667 12 3.701 14 3.708 16 3.70867
The following is HPLC data. Using the standard curve determine the concentration of caffeine in each sample in µg/µl: Sample Peak area Volume of sample Amount of caffeine µg/ µl 1 1305490 1 µl 2 7836463.3 1 µl 3 3476413.7 1 µl 4 2936950.7 1 µl 5 15452894 1 µl 6 958353.7 1 µl 7 592743.3 1 µl 8 557099 1 µl 9 653410.7 1 µl 10 734443.7 1 µl
Calculate the dose in Mg: What is the dose of a patient weighing 30 kg, if the dose is 10 mg/kg?
Explain the relationship between the minimum inhibitory concentrationand the therapeutic index. What is optimum for each?
. At therapeutic range, theophylline follows linear pharmacokinetics. The average t1/2 is 3.4 hours, and the average volume of distribution is 30 L. What is the average clearance for theophylline assuming a one-compartment model?
Prednisone 5mg Quantity: CLXIV 5 tabs po qd x4 d, taper down by one tablet every 5 d for 15 d then ss po qd. how many tablets should be dispensed?
Megadoses of antioxidants are a great way to catch up on deficiencies, and since they are natural, they have no harmful side effects. true or false