Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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- IX. Insulin, a hormone vital in blood sugar regulation and having a polypeptide chain with disulfide linkages, loses its regulatory activity when heated at nearly 100°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of insulin relative to its native structure and function. I--arrow_forwardH8.arrow_forward1. Provide the best coenzyme(s) for each step shown below. Give a 1–2 sentence rationale for your choice. 2. Reaction (C) can require multiple coenzymes, or the enzyme may only require one. Briefly describe how the reaction that uses only one coenzyme works. Be specific about the mechanism.arrow_forward
- 21. The apparatus below was used to investigate anaerobic respiration:- release cess can ion: 2830kJ Energy rtially en to anol). ent in --110 Glucose solution and yeast Suspension Lime water (a) How would you remove dissolved oxygen from the glucose before the experiment commencing? (b) State what happens to the lime water as the experiment proceeds to the end (c) Describe the reactions in the experiment xplain what would happen if the temperature of glucose solution and yeast was raised eyond 45°C ition d as is ndarrow_forward48arrow_forward47. The transfer of Energy and subsequent production of ATP (cellular respiration) is actually a(n). the breakdown of Glucose, which is energetically, rxn. However, the reaction requires Bles Yourn a. endergonic : exergonic b. exergonic : endergonic c. catabolic : neutral d. dehydration : unstablearrow_forward
- please focus on this question 3 times i submitted it and three different answers, please make sure of ur answerarrow_forward45. Which of the following is/are true? (MARK ALL THAT APPLY) Group of answer choices Enzymes lower the activation energy of the reaction Enzymes bind more strongly to the substrates than the transition state of the reaction Enzymes alter the standard free energy of the reaction. Enzymes force reactions to proceed in only one direction. Enzymes alter the equilibrium of the reaction. PreviousNextarrow_forwardA. How does each of the following irreversible inhibitors interact with the Enzymes? IV. 1. Cyanide 2. Heavy-metal ions B. List an antidote for each of these two poisons and describe how each functions.arrow_forward
- 2. Enzyme-catalyzed reactions. Answer the following with true or false. If false, explain why. (a) The initial rate of an enzyme-catalyzed reaction is independent of substrate concentration. (b) At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. (c) The Michaelis constant Km equals the substrate concentration at which velocity (v) = Vmax/2. (d) The Km for a regulatory enzyme varies with enzyme concentration. (e) If enough substrate is added, the normal Vmax of an enzyme-catalyzed reaction can be attained even in the presence of a noncompetitive inhibitor. (f) The Km of some enzymes may be altered by the presence of metabolites structurally unrelated to the substrate. (g) The rate of an enzyme-catalyzed reaction in the presence of a rate-limiting concentration of substrate decreases with time. (h) The sigmoidal shape of the v versus [S] curve for some regulatory enzymes indicates that affinity of the enzyme for the…arrow_forward20) Normally an enzyme has maximal enzyme activity at 37°C, but once it has been heated to 100°C and then cooled back down to 37°C the enzyme is no longer active. Why?arrow_forward12. Explain why those biological reactions that have their equilibria shifted towards theproducts have negative values for ΔGo of reactions. Explain how equilibria relates toGibbs free energy.arrow_forward
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