What kind of quality assessment is performed on amylase and why is this important? 2. What are the advantages and disadvantages to using amylase?
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1. What kind of quality assessment is performed on amylase and why is this important?
2. What are the advantages and disadvantages to using amylase?
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- 1. What are the primary tissue sources of amylase? 2. What is the clinical significance of increase serum amylase activity? 3. What are the assay methodologies? Describe each.1. Draw and label completely the electrophoretic pattern of CK isoenzymes 2. What are the sources of error in Amylase determination?1. In zero order reaction, the reaction rate depends only on enzyme concentration. In first order reaction the reaction rate is directly porportional to substyrate concentration a. first statement is false and second statement is true b. both statement is true c. both statement is false d. first statement is true and second statement is false 2. These are catalyst that can be used in the monitoring and diagnosis of disease and their remarkable properties make them sensitive indicators of pathologic changes. a. enzymes b. electrolytes c. substrate d. none of these 3. ALT is stavle in serum at refrigirator or temp for up to 3 weeks, indefinitely if frozen AST has the same stability but markedly decreases with freezing a. both statement are true b. both statement are false c. first statement is true second is false d. second statement is true first statement is false
- 6. When a concentrated alkali solution acts on the purine cycle, it breaks down: A. Ester group B. Imidazole nucleus C. Dioxopyrimidine nucleus D. Lactone cycle 7. According to the Pharmacopoeia, sodium thiopental is quantitatively determined by the following methods: A. Acidimetry B. Alkaimetry C. Gravimetry D. HPLC E. UV spectroscopy 8. When determining the content of free alkali in sodium salts of barbiturates, an indicator is used: A. Methyl orange B. Methyl red C. Timolphthalein D. Phenolphthalein 9. NH-acidic properties are shown by: A. Sulfacyl sodium B. Sodium barbital C. Theobromine D. Hexamidine (primidone) 10. Derivatives of pyrimidine-2,4-dione are derivatives: A. Uracil B. Uretane C. Barbituric acid D. Malonic acid 11. The cerimetric method can be used for quantitative analysis: A. Nicotinic acid B. Atropine sulfate C. Gomatropin hydrobromide D. Nicotinic acid diethylamide E. Nifedipin1. Describe the specificity of glucose oxidase. Compare it with the three other methods.1.Why do you think glutathione occurs in a concentration as high as glucose? 2.Explain why glutathione must be transported from cytosol to mitochondria. 3.Explain why glutathione can confer therapeutic benefit when taken orally.
- 1. Explain how temperature and pH affect enzyme activity from a biochemical standpoint. What are the changes in enzymes caused by these physical factors? 2. Enzymes perform best at 37C, which is the average cell temperature. What does this say about the significance of controlling one's body temperature?1. What is the action of invertase? 2. What is the reagent used to detect glucose in the detection of invertase? What is its principle?1. What is koji and how is it used and prepared as starter enzyme in certain production of food products? list some of its application. (2 pts.) 2. Draw a schematic diagram/process flow diagram of the following enzyme prepared products: Indicate the microorganism used to make the process. (Reminder: Topic is enzyme, here you are applying enzyme-producing microorganisms to produce food/beverage products) 2.1 soy sauce (2 pts) 2.2 miso (2 pts) 2.3 sake (2 pts) 2.4 OTHER PRODUCT YOU CAN FIND involving enzyme preparation (3 pts) 3. Write the chemical reaction involve or show chemical reaction mechanism in(for) the production of the following: (Reminder: deduce the basic chemical reaction, don't provide complex reaction mechanism(s). Quiz will not give you a complex reaction :) 3.1 soy sauce (3 pts) 3.2 miso (3 pts) 3.3 sake (3 pts)
- 1. The Fehling’s reaction, which is a simple assay for reducing sugars, was used as a diagnostic test for the determination of blood glucose concentrations for a very long time. However, it has now been replaced by the glucose oxidase test. The enzyme glucose oxidase isolated from the mold Penicillium notatum catalyzes the oxidation of β-D-glucose to D-glucono-δ-lactone. This enzyme is highly specific for the β-anomer of glucose and does not affect the α-anomer. In spite of this specificity, the reaction catalyzed by glucose oxidase is commonly used in a clinical assay for total blood glucose—that is, for solutions consisting of a mixture of β- and α-D-glucose. Explain how this is possible. Aside from allowing the detection of smaller quantities of glucose, what advantage does glucose oxidase offer over Fehling’s reagent for the determination of blood glucose? 2. Consider only the oxygen levels present in the cytoplasm and ECF as shown in the drawing above (no new oxygen is entering…7. Fill in the blank with the correct terms. Phosphorylation and dephosphorylation are what type of enzyme regulation methods? а. Type of non-permanent enzyme inhibition that does not directly interfere with the enzymes active site. Class of enzyme that hydrolyzes esters, amides, and phosphoesters. C. Name of an enzyme that would catalyze the removal of hydrogen from alcohols (product would be an aldehyde). d. Rank the energy bearing phosphate compounds AMP, ATP, and ADP from the citric acid cycle in order of highest energy to lowest. b. e.5. Richner-Hanhart syndrome is associated with a defect in which of the following? A. Fumarylacetoacetate hydrolase B. Tyrosine aminotransferase C. p-hydroxyphenylpyruvate hydroxylase D. Homogentisate oxidase