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1. Explain chemotherapy in terms of specific inhibition
2. Explain why enzyme activity declines at (a)high temperature and (b) presence of heavy metal ions.
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- 6. Explain the basis of enzyme replacement therapyExplain chemotherapy in terms of specific inhibitionCompetitive Inhibition,Noncompetitive Inhibition, and Uncompetitive Inhibition1.State the principle that underlies the following biochemical tests: a) Methyl red testb) Voges-Proskauer test 2. how does oxidative phosphorylation differ from substrate-level phosphorylation?
- Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme. b. If an inhibitor binds the active site, it is considered noncompetitive. c. If an inhibitor binds to a site other than the active site, this competitive inhibition. d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable. e. Competitive inhibition is usually not reversible.1. Give the importance of carbohydrate fermentation test in biochemical testing and enumerate the enzymes that are involved. 2. What are the substances added in the culture media utilized by the organism producing hydrogen sulfide? Give 2 other media used for the production of hydrogen sulfide. 3. Explain the mechanism taking place in the hydrolysis of urea which leads to the formation of bluish red color. 4. Discuss why human blood plasma will not always yield reliable results.9) Considering the enzymatic reaction catalyzed by HIV protease: Options A) hydrolysis is the net reaction observed. B) a peptide bond is cleaved on the carboxyl side of a proline residue. C) a serine residue serves as the nucleophile during the catalytic event. D) inhibitors have been designed to covalently link to the active site just like natural substrates do. E) None of the above is true. F) All of the above are true.
- 2. Explain why enzyme activity declines at (a)high temperature and (b) presence of heavy metal ions.2. an enzyme-catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained. (S)[M] V (umol/min) V (+inhibitor)(umol/min) 6 x 10-6 20.8 12 1 x 10-5 29 15 2 x 10-5 45 20 6 x 10-5 67.6 24 1.8 x 10-4 87 28 plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reaction and reaction with inhibitor. Use the same graph for both plots. calculate the Km of enzyme in the reaction without inhibitor Km1 of the enzyme in the reaction with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction what kind of inhibitor was added to the enzyme-catalyzed reaction? explain your answer in terms of changes in Km and Vmax.21) a decrease in cell mass, reduction, is observed when which of the following conditions are met. a) abundant energy b) abundant amino acids c)growth factors d) all of these e)none of these
- In vitro conditions the enzyme is used in catalytic amounts (10-12 to 10-8M). Estimate the amount of enzyme in living cell. Assuming (a) fresh tissue is 80% water and intracellular (b) total soluble protein in cell represents 15% of wet weight (c) all soluble proteins are enzymes (d) average molecular weight of protein is 150,000 (e) about 1000 different enzymes are present.1. Describe the specificity of glucose oxidase. Compare it with the three other methods.1. Explain the biochemical formation of creatinine, urea, and uric acid. 2. State the principle of the Jaffe (end-point, and kinetic) and the enzymatic methods for measuring creatine.