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Clinical Chemistry 2: Enzyme Kinetics
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Clinical Chemistry 2: Enzyme Kinetics

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Questions and Answers

What is the primary advantage of measuring the increase in product rather than the decrease in substrate in enzyme reactions?

  • The increase in product is a direct measure of enzyme activity
  • The decrease in substrate is a slower process
  • It is easier to measure the increase in product (correct)
  • It is easier to measure the decrease in substrate
  • What is the effect of increasing the ionic strength of a solution on enzyme activity?

  • It depends on the type of enzyme
  • It has no effect on the enzyme activity
  • It increases the enzyme activity
  • It decreases the enzyme activity (correct)
  • Which of the following is NOT a suitable anticoagulant for measuring enzyme activity in a blood sample?

  • EDTA (correct)
  • Citrate
  • Heparin
  • Oxalate
  • What is the effect of a 10°C increase in temperature on enzyme activity?

    <p>It causes a doubling of enzyme activity</p> Signup and view all the answers

    What type of enzyme inhibitor competes with the substrate for binding to the active site of the enzyme?

    <p>Competitive inhibitor</p> Signup and view all the answers

    What is the pH range in which most enzyme reactions occur?

    <p>pH 7-8</p> Signup and view all the answers

    What type of inhibitor binds to an enzyme different from the catalytic site, removing cofactors in the process?

    <p>Non-competitive inhibitor</p> Signup and view all the answers

    Which class of enzyme catalyzes the transfer of a group, other than hydrogen, from one substrate to another?

    <p>Transferase</p> Signup and view all the answers

    What is the purpose of the last number in the Enzyme Commission of the International Union of Biochemistry standardized designation?

    <p>To indicate the specific number given to each enzyme in its sub-subclass</p> Signup and view all the answers

    What type of enzyme catalyzes the removal of groups from substrates without hydrolysis, resulting in a double bond product?

    <p>Lyase</p> Signup and view all the answers

    What is the function of an uncompetitive inhibitor?

    <p>To bind to the E-S complex and prevent dissociation</p> Signup and view all the answers

    What is the primary function of ligase enzymes?

    <p>To catalyze the joining of two substrate molecules coupled with the breaking of a pyrophosphate bond</p> Signup and view all the answers

    What is the primary advantage of using Alanine Aminotransferase (ALT) over Aspartate Aminotransferase (AST) in diagnosing liver disease?

    <p>ALT is more specific to liver disease</p> Signup and view all the answers

    Which of the following methods is used to detect Alanine Aminotransferase (ALT) activity?

    <p>Reitman-Frankel method</p> Signup and view all the answers

    What is the main difference between the substrate used in the Bodansky method and the Shinowara Jones method?

    <p>One uses beta-gycerolPO4, while the other uses beta-glyceroPO4</p> Signup and view all the answers

    Why do ALT elevations tend to remain longer than AST elevations in acute inflammatory conditions of the liver?

    <p>ALT has a longer half-life in serum</p> Signup and view all the answers

    What is the primary concern when measuring ALT activity in patients with viral hepatitis?

    <p>Hemolysis of red blood cells</p> Signup and view all the answers

    Which of the following is a characteristic of AST that distinguishes it from ALT?

    <p>Higher concentration in heart</p> Signup and view all the answers

    What is the effect on reaction speed when the substrate concentration is doubled in a first-order reaction?

    <p>The reaction speed is doubled</p> Signup and view all the answers

    Which type of inhibitor binds to the active site of the enzyme?

    <p>Competitive inhibitor</p> Signup and view all the answers

    What is the unit of enzyme activity that represents the amount of enzyme needed to catalyze the conversion of 1 mole of substrate to products per second?

    <p>Katal</p> Signup and view all the answers

    What is the conversion rate of 1 IU to kat?

    <p>1 IU = 16.7 kat</p> Signup and view all the answers

    What is the method of measuring enzyme activity that involves measuring the rate of disappearance of substrate per unit time?

    <p>Measuring the rate of disappearance of substrate per unit time</p> Signup and view all the answers

    What is the term for the substrate that is acted upon by the enzyme and is incubated with enzymes present in the patient's serum?

    <p>Substrate</p> Signup and view all the answers

    What is the primary reason for separating serum from clot quickly in LD isoenzyme measurement?

    <p>To prevent increase in LD1 and LD2</p> Signup and view all the answers

    In which condition is a flipped pattern of LD1 > LD2 typically observed?

    <p>Cardiac necrosis</p> Signup and view all the answers

    What is the primary isoenzyme fraction in the sera of healthy individuals?

    <p>LD2</p> Signup and view all the answers

    Which of the following isoenzymes is NOT typically used to test liver disorders?

    <p>LD3</p> Signup and view all the answers

    What is the primary reason for avoiding hemolysis in LD isoenzyme measurement?

    <p>To prevent LD1 and LD2 elevation</p> Signup and view all the answers

    What is the primary characteristic of LD5 isoenzyme in terms of temperature?

    <p>Cold-labile</p> Signup and view all the answers

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