1. Describe the accuracy and specificity of Nelson-Somogyi method 2. Do you think PFF should be part of enzymatic method of glucose determination? Explain your answer.
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1. Describe the accuracy and specificity of Nelson-Somogyi method
2. Do you think PFF should be part of enzymatic method of glucose determination? Explain your answer.
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- 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.1. Describe the specificity of glucose oxidase. Compare it with the three other methods.1. Suppose the following kinetic data was collected for an enzymatic reaction For each substrate concentration, calculate and show the average initial rate and its standard deviation. [substrate), mM initial rate, min¹ Average initial rate, min¹ 150 62 150 60 150 63 40 44 40 41 40 43 222 12 11 15 Calculation of rates (min) for acid phosphatase reaction General Procedure for the End Point Assay of What Germ Acid Phosphate The general procedure used for each assay except the concentration of p-nitrophenyl phosphate was varied. The concentration of acid phosphatase was 7.2 μM) and each assay involve a 5-minute incubations with enzyme. Using this information along with the extinction coefficient of the p- nitrophenol product of the reaction allows for the initial rate to be expressed in terms of min¹. Vo [E] = absorbance at 410 nm 0.677 = initial rate in min-1
- answer the following questioms.. 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?2Cemical analysis of a patient’s urine using a reagent strip gave negative protein and negative glucose results. However, using a separate microalbumin reagent strip, the result was positive. Earlier in the day, the urine controls gave the expected results with both types of reagent strips. 1. Is there a discrepancy in the patient’s test results obtained with the two strips? 2.Should the urine chemistry controls be rerun? 3.What is the most likely explanation for the results?1. Give the importance of carbohydrate fermentation test in biochemical testing and enumerate the enzymes that are involved. (5 points) 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. (5 points) 3. Explain the mechanism taking place in the hydrolysis of urea which leads to the formation of bluish red color. ( 5 points) 4. Discuss why human blood plasma will not always yield reliable results. (5 points)
- Match the chemical reaction to the visual effect of the product/biochemical test description 1. This assay's color change relies on an initial reduction reaction resulting in a black precipitate if the organisms is "positive" 2. The visual production of gas from this reaction indicates this organism can break down toxic byproducts of aerobic respiration. 3. This assay relies on a pH indicator (phenol red) for a color change. An organism that was "positive" for the certain enzyme in this assay, would result in a pink color change. 4. If an organism was incubated in simple broth containing a phenol red pH indicator and a sugar source, and the broth turned yellow following bacterial growth, that would be evidence of this reaction occurring. 5. The reaction representing this assay, works by producing a red colored product upon addition of a reagent, which tells us the organism possesses the enzyme required to break down a particular amino acid.Description of clinical trial process for the Pfizer-BioNTech. Incorporate the following key words: Length of trial; population diversity; efficacy; side effects Pfizer-BioNTech11. 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.
- 5. The data in the table below were collected during a laboratory session assaying for thekinetics of Acid Phosphatase. Using a simple flow diagram, show how you would design theexperiment and focus on the principles of the assay and the major components for theexperimental design. Concentration (mM) Absorbance1 (410nm) Absorbance2 (410nm)0 0.007 0.0081 0.051 0.0672 0.078 0.0965 0.168 0.1558 0.234 0.25210 0.297 0.31620 0.523 0.514 30 0.759 0.719a. From experimental data obtained in Figure 1, construct a plot and equation that determines the rate constant, kM, of the MOX activity in conditions A and B of growth culture of H. polymorpha on methanol. Justify the selection of plot and findings. b. From the data behaviour presented in Figure 1, describe the enzymatic activity of MOX. What factors may influence the enzymatic activity of MOX at different condition batch cultures of H. polymorpha.Q1. WHY IS IT NOT ADVISABLE TO MOVE/ TOUCH THE AGAROSE GEL IN THE PROCESS OF HARDENING. Q2. WHAT IS THE USE OR FUNCTION OF THE TAE BUFFER THAT IS POURED THE GEL OR FOUND IN THE GEL BOX. Q3. HOW CAN YOU TELL IF A GEL IS RUNNING? Q4. OUTLINE THE PROCESSES USED IN THE PREPARATION OF AGAROSE GEL OF 1.5CONCENTRATION. Q5. OUTLINE THE PROCEDURE/STEPS USED IN GEL ELECTROPHORESIS( please don’t copy from the Internet, write in your own words the process of the experiment. ) Q6. NAME TWO EXAMPLES OF THE DYE USED IN GEL ELECTROPHORESIS. Q7. HOW DO WE PREPARE ×1(concentration) TAE BUFFER FORM 50× TAE BUFFER .