elearn.squ.edu.om/mod/quiystem (Academic)The enzyme asparaginase is used to reduce the level of asparagine in blood in the treatment of leukemia.Which of the following forms of Asparaginase would be most useful if the blood asparagine level is 0.2 mM?Select one:O a. Km = 2.0 mM; Vmax = 0.1 mM/hourO b. Km = 0.1 mM; Vmax = 0.5 mM/hour%3DО с. Кm0.2 mM; Vmax = 0.1 mM/hourO d. Km = 0.1 mM; Vmax = 0.1 mM/hourO e. Km = 0.2 mM; Vmax = 0.5 mM/hourClear my choiceIn a steady state (of ES formation and ES breakdown)Select one:a The rate of formation of ES is equal to the rate of its degradation during the reaction

According to Michaelis Menton kinetics of enzyme, Km is substrate concentration at half Vmax where…

Answered: The enzyme asparaginase is used to…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Which of the following is true regarding folate/folic acid: a.Intakes below recommended dietary allowance (RDA) during pregnancy is associated with neural tube defects b.Excess intakes of folic acid (above UL) should be encouraged as there are no associated adverse effects c.Intakes above the tolerable upper intake levels (UL) of 1000 µg/day should be avoided because it may lead to adverse health effects, including masking B-12 deficiency d.a, c
Sarin (chemical name: propan-2-yl methylphosphonofluoridate) is considered a weapon of mass destruction by the United Nations by virtue of its ability to kill with great efficiency in very low concentrations. a. Chemicals with action similar to Sarin, such as Neostigmine (drug names: Prostigmin, Vagostigmin) have great clinical utility. For what conditions has the drug been approved for treatment by the U.S. Food and Drug Administration? b. Describe the mechanism of action whereby the application of properly dosed Neostigmine ease the symptoms of the disorder.
There are two types of antifolate drugs (primarily DHFR inhibitors): Classical antifolates and Non-classical antifolates. How do these two types of antifolates differ from each other? a.Mode of transport into the cell b.Natural vs synthetic c.Function
What would the order of elution be (first to last to come out of a size-exclusion chromatography column) for the mixture of myoglobin (17.7 kDa), hemoglobin (64.5 kDa), lysozyme (14.3 kDa) & albumin (67 kDa)? a. Albumin, hemoglobin, lysozyme, myoglobin Ob. Hemoglobin, myoglobin, lysozyme, albumin Oc. Lysozyme, myoglobin, albumin, hemoglobin Od. Albumin, hemoglobin, myoglobin, lysozyme
The above photo is that of a leukemia patient 24 hours after receipt of a bone marrow transfusion. 1. What is the name given to this reaction and what causes it? 2. How is this condition graded? 3. This reaction can provide a benefit to the recipient. Explain. 4. If a sister donates hematopoietic stem cells to her brother what might result and why?
Given the following, calculate Gk: ENa = +45 mV; Ek = -85 mV; ECl = -60 mV; GNa = 5x10-8 S; GCl =0; Vm = -70 mV
(e) Two ADP agonists (drugs) were also found to bind to platelets: 2-methylthio-ADP bound with a Kp of 7 µM and 2-(3-aminopropylthio)-ADP bound with a Kp of 200 µM. Can these drugs effectively compete with ADP for binding to platelets? Explain your answer.
Normal Hgb is referred to as HbA and contains 4 subunits, 2 a-globin chains and 2 B-globin chains, arranged as two dimers of aß. In Sickle Cell Disease, both B-globin chains are altered in the dimers (aßS/aßS). Q3: Which level of structure does the aß/aß and aßS/aßS in HbA and HbS describe?
If there was a molecule that causes Hb to be more stable in the T state, this molecule would: a. Generally, raise the affinity of Hb for O2 b. Generally, lower the affinity of Hb for O2 c. Generally, cause Mb to favor the R state while Hb is in the T state d. Generally, cause Hb to dissociate into αβ dimers
People suffering with sickle cell anemia have a structural defect in hemoglobin (HB). The major reason for this structural change is mutation of glutamic acid to valine. This leads to a Exposure of polar amino acids, leading to disintegration of hemoglobin. b Burying of polar amino acids, leading to disintegration of hemoglobin. c Exposure of non-polar amino acids leading to long fiber formation. d Burying of non-polar amino acids thereby increasing hydrophobic interactions and formation of long fibres.

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