7.0, each into e 2 in ne ding 1. Du kan 8 10 6 itions. TABLE 2 Effect of pH on the Hydrolysis of Starch Time (Minutes) 3.0 7.0 0 73 73ba73 W 73 73 1.930 73 73 73 2 4 73 73 73 73 73 7 ining buffered enzyme 11.0 3 1,070 0.747 مرد
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- 12 Avdil DiC diLei OcL 27 dl 1.Jopm nents Enzyme Reaction Rates ts prary racker 10 20 30 40 50 2 4 6. 8. 10 Temperature (°C) pH Based on these data, this enzyme functions best at what temperature and pH? Remind O Temperature of 27°C and a pH of 4 O Temperature of 40°C and a pH of 8 Four O Temperature of 50°C and a pH of 10 Calculator O Temperature of 37°C and a pH of 6Enzyme kinteics of amylase using l2 in KI was used to determine starch conc at t = 0 min and t = 1 min. Tubes were set absorbance measured after 1 minute of incubation. The reaction was halted with HCl and 5 mL of I, in KI indicator was added. 1 ml of each was used as sample in the spectrophotometer. Using this table, Concentration of Volume of Volume of Volume of l2 Test tube stock starch, in KI solution, Absorbance starch solution, mL water, mL distilled mg/mL mL 1 10 5 0.0009 2 10 0.4 4.6 0.3306 3 10 0.8 4.2 0.5891 4 10 |1.2 3.8 0.8409 5 10 1.6 3.4 1.0885 6. 10 2.0 3.0 1.2572 What is the standard curve for the conc. of the starch?Enzyme kinteics of amylase using l2 in Kl was used to determine starch conc at t = 0 min and t = 1 min. Tubes were set absorbance measured after 1 minute of incubation. The reaction was halted with HCl and 5 mL of I, in KI indicator was added. 1 ml of each was used as sample in the spectrophotometer. Using this table, Concentration of Volume of Volume of Volume of l2 Test tube stock starch, starch distilled in KI solution, Absorbance mg/mL solution, mL water, mL mL 1 10 0.0009 2 10 0.4 4.6 5 0.3306 3 10 0.8 4.2 0.5891 10 |1.2 3.8 0.8409 10 |1.6 3.4 1.0885 10 2.0 3.0 1.2572 What is the standard curve for the conc. of the starch?
- please fill out the table I need it for lab tomorrow At the start of the lab, you will be given stock preparations of alkaline phosphatase and PNPP onice—keep them that way. You will also be instructed on the volume of enzyme solution to beadded to reaction mixtures. Typically, this lab uses 5 μl of enzyme dilution. Before the start of lab, calculate thevolumes in μl of each component you need to mix together for each of these samples.For all of the following assays, use the amount of enzyme noted above and vary the substrateconcentration. Use the following assay format and PNPP concentrations of 0.0, 0.20, 0.40, 0.60,0.80, and 1.0 mM. Calculate the volumes of the 100 mM PNPP stock solution and buffer (finalvolume of 1.00 ml) needed to get each of the substrate concentrations. A single blank tube, withalkaline buffer only, is sufficient, because PNPP has no absorbance at 405 nm.OSTATES OF MATTER Finding mass or volume from percent concentration To my home Com GED Math Pract Ketamine, sometimes used as an adjuvant to general anesthesia, is available as a 1.0 %(w/v) solution. Calculate the volume of this solution that contains 20 mg of ketamine. Be sure your answer has a unit symbol and is rounded to the correct number of significant digits.Calculate your dilution strategyto make a 625 ng/mLHRP solution from a 12.5 μg/mL stock given the totalvolume of enzyme youwillneed for your condition this week. Note if you are testing pH, you only need to calculate one enzyme dilution because all other pHs will use the same strategy.
- Ib 20 n moles OL produch ane observed In 10 minutes and 50 nmoles 20 minutes obsenved is Vo? product in are then cwhat8 7- 6- 2- 1- 45 90 135 180 225 270 315 360 405 450 495 540 58! [Substrate] (nM) What is the Vmax of the enzyme data shown above? rate (nM/sec) 3.Pepsin, a peptidase that hydrolyzes proteins, functions in the stomach at an optimum pH of 1.5–2.0. How is the rate of a pepsin-catalyzed reaction affected by each of thefollowing conditions? increasing the concentration ofproteins changing the pH to0 running the reaction at 0°C using lesspepsin
- 46 2 H 8 Is M (n Ge M In In VI LE Q s M In b M 7 x + uv A canvas.northseattle.edu/courses/2086259/quizzes/5876542/take (a) Saturated fatty acid (b) Unsaturated fatty acid Account Dashboard Palmitic acid Linoleic acid 200L anauer Aemciates Ine. Courses Shown here are examples of saturated and unsaturated fatty acids. Explain what is meant by the term saturated fatty acid, and explain, at the molecular level, why Groups saturated fatty acids remain solid at higher temperatures than unsaturated acids do. Calendar Edit View Insert Format Tools Table В T? v: 12pt v Paragraph v U A Inbox History Help 8:18A technician prepares a buffer solution that will be used to facilitate the optimal pH for an enzyme involved in the biotechnological degradation of organic compounds. The buffer compound will facilitate a stable pH. To prepare the buffer they need to determine the required concentration of anita hara [conjugate acid or base]_08 They have been provided with the buffer parameters provided in the images. Provide the answer to three decimal places and include an appropriate unit. Note: You may need to round the numbers to get the required answer. Final volume of solution: 200 ml VEENER Total buffer compound concentration: 150 mM Ratio conjugate base/weak acid: 1.58/1 2000 Concentration weak acid: 0.058 M Final pH of solution: 6.5 Buffer compound pk.: 6.3 14 13 12 11 10 9DQuestion 21 GC and HPLC were used in this course as: O synthetic techniques analytic techniques purification techniques O liquid-liquid extraction techniques D Question 22 Based on the boiling point of acetone (56° C), 3-methylbutylacetate (141°C), and 3-methyl-1- butanol (131°C), which compound will be the first to come off (elute) the GC column? O acetone O 3-methylbutylacetate O 3-methyl-1-butanol