Typical activity curves of enzymes that are analyzed in the test tube, like the one presented below, flatten out with time. Provide two possible reasons why this is observed. Must be less than 50 words total

Typical activity curves of enzymes that are analyzed in the test tube, like the one presented below, flatten out with time. Provide two possible reasons why this is observed. Must be less than 50 words total

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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For the study of alanine production by a recombinant strain of E. coli, cultivation was carried out in a benchtop bioreactor with 4.5 L of culture medium, using glucose as a limiting substrate. During the cultivation, there was no lag phase and the cells showed exponential growth for 5 hours. The following table presents the results of the analysis of ammonia and glucose consumption, and alanine accumulation throughout the cultivation. Knowing that 500 mL of a cell suspension at a concentration of 5.0 g/L (inoculum) was added to the 4.5 L of medium in the reactor and that the YX/NH3 previously determined was 7.5, calculate:a) the maximum specific growth rateb) YX/S and YP/S yield factorsc) How long would it take to reach Cx = 30 g/L if the cells continued with the exponential growth profile until the end of the culture (without nutrient deprivation or any type of inhibition)?d) Describe how the mathematical treatment of the data should be done to determine the type of product formation…
Is the following statement correct or incorrect? It is only possible to employ enzymes that are present naturally in yeast or bacteria for biocatalysis.
Two-dimensional gel electrophoresis of proteins in a cell extract provides a qualitative way to compare proteins with respect to intra- cellular abundance. Describe a quantitative approach to the deter- mination of number of molecules of an enzyme per cell.
You design an enzyme assay and choose a substrate concentration equal to the Km of the enzymatic reaction. You measure the rate of the reaction at this substrate concentration to be 75.0 μmol/min. Calculate the Vmax of this reaction in μmol/min. Express your answer with one decimal place. Your previous attempt suffered from low signal-to-noise ratio when you used a substrate concentration equal to the Km. So you decide to increase the substrate concentration to 0.45 mM. You remeasure the rate of the reaction at this new substrate concentration and find it to be 135.0 μmol/min. Using the same Vmax value found above, calculate the Km value of this enzymatic reaction. Express your answer in μM with one decimal place. Considering the previous two questions, what would be the rate of the reaction at a substrate concentration of 0.01 mM? Express your answer in μmol/min with one decimal place.
This is my data collected from a Succinate Dehyrogenase Enzyme Assay - I am asked to plot a Concentration vs Time while plotting the Resuspended and Supernatant Reaction; how can this be completed? Test Tube Concentration (uM) Absorbance @ 600nm #1 0 0.00 #2 5 0.090 #3 10 0.187 #4 20 0.368 #5 40 0.715 #6 60 1.075 Table 3. Succinate Dehydrogenase Assay @ 600 nm Time point (min): Resuspended Pellet Reaction Absorbance Supernatant Reaction Absorbance Enzyme Reaction Control Absorbance 0 43.2 44.2 46.1 3 43.3 44.8 6 43.0 44.9 9 42.6 45.2 12 43.5 45.6 15 44.0 45.7 18 43.8 45.9 21 44.0 46.4 24 44.1 46.5 27 43.9 46.7 30 43.7 46.9 43.6
If 10 µM enzyme was used to obtain the data in the summary plot below, k-cat = ________________ sec-1 and efficiency = _________________ sec-1 M-1 for this enzyme. (Enter numeric answers to the nearest integer; Do NOT write unts.)
A protein (PrX) was heated in vitro to 45C for 15 min, in the presence or absence of Hsp40, Hsc70, and ATP. The amount of PrX in aggregated (P, pellet) and soluble (S) fractions was then quantified (Bars, 1 SD). Based on these data, answer the following questions. In all cases, give brief justification for your answer. a) How does Hsp40 alone influence the solubility of PrX? b) How does Hsc70 alone influence the solubility of PrX? c) Do Hsp40 and Hsc70 co-operate in this experiment? d) Which components combined provide maximal solubility of PrX after heat shock?