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- 1.How is acid or alkaline detected in a culture medium as an end product? 1.The tests for the hydrolysis of starch, casein, and triglycerides are similar in terms of setup . How do the methods for the detection of hydrolysis differ between these three tests?1. What is the purpose of the different reagents used in the procedure of kato-katz technique? 2. How are the Kato Katz Technique results reported? 3. What are the advantages and disadvantages of using Kato-Katz Technique?11. The most highly sensitive test in viral hepatitis is y-Glutamyl transpeptidase (Y-GT) increased activity in blood, which level riscs 10-15 times more than the norm (30-50 ME/L). What is the diagnostic value of this enzyme? For the answer: a) present the main properties of enzymes which activity determination in patient blood are widely uscd in enzyme diagnostics; b) explain the y-Glutamyl transpeptidase (y-GT) system and present an appropriate scheme; c) give examples of other enzymes which activity is determined in the liver disorders.
- 1. How does the resin facilitate purification in glutathione S-tranferase (GST) affinity? 2. Does protein stick to the resin in glutathione S-tranferase (GST) affinity? If so how do you get it off? 3. Explain how protein of interest would be purified in glutathione S-tranferase (GST) affinity?1. Explain the Biochemical method to identify E.Coli1. Is the reagent used to cut peptide bonds during amino acid analysis. 2. Is the name of the amino acid present in the active site of carbonic anhydrase. 3. Is the name of the reagent used to poison serine proteases. Is a component of bacterial cell wall other than N-acetylglucosamine? 4. 5. Is the optimal pH of lysozyme.
- Lysosyme catalyzes the hydrolysis of the carbohydrate linkage in part of the bacterial cell wall (peptidoglycan layer). 1. Propose a mechanism using general acid/base catalysis 2. Propose a mechanism using covalent catalysis. (An intermediate has been observed that indicates a glycosidic bond to the aspartate).Gelatin Hydrolase: 1. Explain the incubation conditions 2. Explain the reagents being added 3. Explain the observations in Gelatin Hydrolase 4. Explain the interpretations in Gelatin HydrolaseEx. 5-4 Catalase 1) In the Catalase test (5-4), if bacteria was added to hydrogen peroxide on the slide, it might produce a false result. 2) Explain why adding bacteria to the hydrogen peroxide on a slide rather than adding the hydrogen peroxide to the bacteria on the slide might give a false result? 3) Would the false result be a false positive or would the false result be a false negative?
- 2. During SDS PAGE, Tighnari loaded the purified protein extract from redcrest and padisarah, another sample that he is working with for his dissertation. Note that the isolated proteins from padisarah have molecular weights similar to that of the proteins isolated from redcrest. The results of the SDS-PAGE are shown in Figure D.2. SDS-PAGE w/o ß-mercaptoethanol LANE 1 B D LANE 2 PHILGAR SDS-PAGE w/ p-mercaptoethanol LANE 1 !!! LANE 2 Figure D.2. Electrophoretogram obtained after SDS-PAGE of the purified protein extract from redcrest and padisarah.Non-enzymatic browning Proteins: Lysin, methionine Sugars: glucose, galactose, sucrose, fructose, maltose 1. Describe (the aromas produced) and the degree of browning for each solution 2. Explain variations in color with respect to each sugar-amino acid combination by taking the chemical structures of sugars and amino acids into consideration6. A solution made up of 500 mL of 50% dextrose, 500 mL of 8.5% Aminosyn, and 300mL of sterile water for injection is ordered. a) What is the total weight (in grams) of the dextrose? b) What is the total weight (in grams) of Aminosyn? c) 20 mEq of KCI are needed in the infusion above. How many mL of KCI should be added? Stock strength available: KCl 2 mEq/mL d) 22 mEq of NaCl are also needed in the infusion. What volume of NaCl should be added? Stock strength available: NaCl 4.4 mEq/mL e) What is the total volume of solution with the original fluids and the addition of KCI and NaCl?