Exam 14: Enzyme and Rate Analyses

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The interaction of the amino acid side chains with the arrangement of the α\alpha -helices and β\beta -sheets to form a three-dimensional protein structure is called the _____ structure of the protein.

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An example of a posttranslational modification of an enzyme that produces an enzyme isoform would be:

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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?

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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:

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In a continuous-monitoring assessment of an enzyme reaction rate,which one of the following is the preferable measurement?

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In regard to the expression of enzyme activity,a katal is:

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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.

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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:

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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:

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How does pH alter an enzymatic reaction rate?

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Which one of the following is a correct statement describing a property of an enzyme?

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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?

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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?

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During embryonic and fetal development,changes in isoenzyme distribution patterns are common.These changes are thought to result from:

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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:

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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:

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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?

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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:

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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:

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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.

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