Exam 14: Enzyme and Rate Analyses
Exam 1: Clinical Chemistry, molecular Diagnostics, and Laboratory Medicine10 Questions
Exam 2: Selection and Analytical Evaluation of Methodswith Statistical Techniques20 Questions
Exam 3: Clinical Evaluation of Methods15 Questions
Exam 4: Evidence-Based Laboratory Medicine15 Questions
Exam 5: Establishment and Use of Reference Values12 Questions
Exam 6: Specimen Collection, processing, and Other Preanalytical Variables21 Questions
Exam 7: Quality Management24 Questions
Exam 8: Principles of Basic Techniques and Laboratory Safety20 Questions
Exam 9: Optical Techniques25 Questions
Exam 10: Electrochemistry and Chemical Sensors15 Questions
Exam 11: Electrophoresis20 Questions
Exam 12: Chromatography17 Questions
Exam 13: Mass Spectrometry13 Questions
Exam 14: Enzyme and Rate Analyses25 Questions
Exam 15: Immunochemical Techniques20 Questions
Exam 16: Automation15 Questions
Exam 17: Point-Of-Care Instrumentation10 Questions
Exam 18: Amino Acids, peptides, and Proteins33 Questions
Exam 19: Serum Enzymes34 Questions
Exam 20: Tumor Markers and Cancer Genes24 Questions
Exam 21: Kidney Function Test-Screatinine, Urea, and Uric Acid17 Questions
Exam 22: Carbohydrates19 Questions
Exam 23: Lipids, lip-Oproteins, apolipoproteins, and Other Cardiac Risk Factors30 Questions
Exam 24: Electrolytes and Blood Gases29 Questions
Exam 25: Hormones15 Questions
Exam 26: Catecholamines and Serotonin23 Questions
Exam 27: Vitamins, Trace Elements, and Nutritional Assessment31 Questions
Exam 28: Hemoglobin, Iron, and Bilirubin25 Questions
Exam 29: Porphyrins and Porphyrias20 Questions
Exam 30: Therapeutic Drugs and Their Management31 Questions
Exam 31: Clinical Toxicology54 Questions
Exam 32: Toxic Metals18 Questions
Exam 33: Diabetes27 Questions
Exam 34: Cardiovascular Disease23 Questions
Exam 35: Kidney Disease25 Questions
Exam 36: Physiology and Disorders of Water,Electrolyte,and Acid-Base Metabolism27 Questions
Exam 37: Liver Disease23 Questions
Exam 38: Gastrointestinal and Pancreatic Diseases20 Questions
Exam 39: Disorders of Bone and Mineral Metabolism25 Questions
Exam 40: Disorders of the Pituitary20 Questions
Exam 41: Disorders of the Adrenal Cortex20 Questions
Exam 42: Thyroid Disorders20 Questions
Exam 43: Reproduction-Related Disorders28 Questions
Exam 44: Pregnancy and Prenatal Testing20 Questions
Exam 45: Newborn Screening and Inborn Errors of Metabolism17 Questions
Exam 46: Pharmacogenetics15 Questions
Exam 47: Principles of Molecular Biology25 Questions
Exam 48: Nucleic Acid Techniques and Applications25 Questions
Exam 49: Genomes and Nucleic Acid Alterations15 Questions
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The interaction of the amino acid side chains with the arrangement of the -helices and -sheets to form a three-dimensional protein structure is called the _____ structure of the protein.
Free
(Multiple Choice)
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Correct Answer:
C
An example of a posttranslational modification of an enzyme that produces an enzyme isoform would be:
Free
(Multiple Choice)
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Correct Answer:
C
The reciprocal plot pictured below indicates a decrease in Vmax and a decrease in Km.The solid line indicates a normal enzymatic reaction.What type of enzymatic inhibition is this?
Free
(Multiple Choice)
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Correct Answer:
C
Varying different factors and studying their effects on an enzymatic reaction rate in the assessment of most favorable reaction conditions for an enzyme assay is referred to as:
(Multiple Choice)
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In a continuous-monitoring assessment of an enzyme reaction rate,which one of the following is the preferable measurement?
(Multiple Choice)
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Zero-order kinetics occurs during the beginning of an enzyme-catalyzed reaction when a substrate concentration is high and the rate of the reaction is _____ on the _____ concentration.
(Multiple Choice)
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Activators increase the rates of enzyme-catalyzed reactions.In some cases,these activators interact with the nonenzymatic component of the reaction such as the substrate.However,in most cases the activator:
(Multiple Choice)
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Immobilized enzymes are used analytically in various electrochemical techniques.The use of an ion-selective electrode that is coated with an enzyme that produces ions when placed in a substrate solution is a type of:
(Multiple Choice)
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Which one of the following is a correct statement describing a property of an enzyme?
(Multiple Choice)
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In the reciprocal plot pictured below,the solid line indicates a normal enzyme reaction with no inhibition,and the dotted line indicates a decrease in Vmax and no change in Km.This plot is an example of which type of inhibition?
(Multiple Choice)
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All enzymes are classified to one of six classes based on the reaction they catalyze.Based on this classification,creatine kinase is a member of which one of the following enzyme classes?
(Multiple Choice)
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During embryonic and fetal development,changes in isoenzyme distribution patterns are common.These changes are thought to result from:
(Multiple Choice)
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Regarding enzyme kinetics,the substrate concentration at which the reaction velocity is equal to 0.5 Vmax is referred to as:
(Multiple Choice)
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When determining the activity of an enzyme in serum as in a bisubstrate reaction,measurement of two different substances can be made.One measurement determines the decrease in substrate concentration acted upon by the enzyme and the other:
(Multiple Choice)
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Regarding enzyme kinetics,the Michaelis-Menten plot of the relationship between reaction velocity and substrate concentration is correctly expressed as which one of the following formulae?
(Multiple Choice)
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In regard to factors that govern the rate of an enzymatic reaction,first-order reaction kinetics occur at that part of the reaction during which the rate of the reaction is:
(Multiple Choice)
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True isoenzymes,which are multiple forms of an enzyme that possesses the ability to catalyze an enzyme's characteristic reaction,are formed by:
(Multiple Choice)
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In an enzyme immunoassay such as ELISA,the specificity of the labeled enzyme is the most important aspect of the measurement.
(True/False)
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