please help i'm stuck A laboratory in Japan performed a similar experiment on earthworms from different localitiesof the Japanese archipelago, but instead of linking trypsin activity within worms to anatomicalfeatures, they were interested in geographical differences in the ability of the worms tobreakdown environmental pollutants using the enzyme polyphenol oxidase. The protocol wassimilar to the one you used, except that enzyme activity was measured from 100 µl of wormextract. Data obtained are displayed below:LocalityReplicate Amount of productConcentration of totalprotein in worm extract(µg/ml)liberated over 10minutes (pmol)Hokkaido11014873310744883589Hon-shu1126221203315644153551194Куu-shu1103429953944108351105Okinawa188329043964100112553From the data in the table, calculate the specific activity of polyphenol oxidase (in units ofumol/min/mg protein) from each locality, presenting the data as mean + standard error (n=5).

Enzyme activity (μmol/min)=Amount of product formed(μmol)time taken(min) Here the amount of product…

Answered: A laboratory in Japan performed a…

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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Using the attachment, Answer the following questions: Prepare a double reciprocal plot with all three experiments (lines) on the same graph. Use your graph, and then answer items 2, 3, and 4 below. 1. Calculate the Vmax or apparent Vmax for all three sets of data. Likewise, calculate the Km or apparent Km for each set. 2. For Inhibitor X, what is the mode/type of inhibition? 3. For Inhibitor Z, what is the mode/type of inhibition? By comparison of the apparent Vmax to the control Vmax, what is the value of α’, as defined in class? If Ki’ = 10 mM for this inhibitor, then what must the inhibitor concentration [Z] be?
To identify the molecule that accepts CO2, Calvin and Benson manipulated the carbon-fixation cycle by either cutting off CO2 or cutting off light from cultures of photosynthetic algae. They then measured the concentrations of various metabolites immediately following the manipulation. How would these experiments help identify the CO2 acceptor? Select one: a. The CO2 acceptor concentration would decrease when the CO2 is cut off, but increase when the light is cut off. b. The CO2 acceptor concentration would increase when the CO2 is cut off, but decrease when the light is cut off. c. The CO2 acceptor concentration would decrease when either the CO2 or light are cut off. d. The CO2 acceptor concentration would increase when either the CO2 or light are cut off.
Pollutants such as halogenated aromatic hydrocarbons (HAHs)are usually spotty in their distributions in bodies of water. Thuseven if HAHs are present, fish might be able to avoid beingexposed to them. Suppose you want to determine if the fishliving in an industrialized harbor are in fact more exposed toHAHs than fish in a more pristine harbor. Why might a study ofliver P450 enzymes be particularly useful for your purposes?
Part a) Which graph has the largest kcat? Please explain. Part b) Which graph has the tightest substrate binding? Please explain. Part c) Which graph has the largest specificity or efficiency constant? Please explain.
In several species of bacteria, GAPDH activity is controlled by the NADH/NAD+ ratio. Does the activity of GAPDH increase or decrease when the NADH/NAD+ ratio increases? Explain. Assume that only the forward direction of the reaction is relevant. a) The activity of GAPDH increases when the NADH/NAD+ ratio increases. b) The activity of GAPDH decreases when the NADH/NAD+ ratio increases.
What is the optimal substrate concentration for the enzymatic reaction presented in the Lineweaver-Burk plot below? a. -0.3211 units/mL b. –3.114 units/mL c. None of these values represent the optimal substrate concentration shown in the Lineweaver-Burk plot d. 3.114 units/mL e. 0.3211 units/mL
A drug with which of the following molecular mechanisms of action would be least likely to function as a DHFR inhibitor? a.Increase DHFR degradation b.Block substrate from binding to the DHFR active site c.Alter folding to increase NADPH cofactor binding
You have isolated a dimeric enzyme that contains two identical active sites. The binding of substrate to one active site decreases the substrate affinity of the other active site. Can the concerted model account for this negative cooperativity?
When ATP and xylose are added to hexokinase, the enzyme produces a small amount of xylose-5-phosphate along with a large amount of ADP. How does this observation support the induced fit model?
Leghemoglobin is a globin protein found in the roots of Legume plants inoculated with Nitrogen fixing bacteria. Leghemoglobin has a binding affinity for oxygen 20 times greater than myoglobin. What function might Leghemoglobin have in the roots of the plant for Nitrogen fixing bacteria? (Hint: The enzyme that catalyzes Nitrogen fixation can also bind O2 , which is not ideal for the enzyme)
A biochemst wants to dtermine the effect of inhibitor on a certain enzyme. See attached data. Using linaer regression analysis, determine the values of Vmax and Km of the enzyme in the absence of an inhibitor 1. y- int ( up to 5 decimal places) 2. slope 3. Vmax 4. Km Using linear regression analysis determine the values of Vmax and Km of the enzyme in the presence of inhibitor 1. y- int ( up to 5 decimal places) 2. slope 3. Vmax 4. Km
State the null and alternative hypotheses, specify the test being used (i.e. two-tail independent Student’s t-test), report the results of the test (include the test statistic, p value, and whether or not you reject the null hypothesis), and relate your findings back to the questions being asked. Seven tomato plants were treated with chlorogenic acid (and seven control plants were not treated) to determine if this acid influences the activity of the enzyme o-diphenol oxidase in their leaves. The enzyme activity data are presented below. Does this treatment affect enzyme activity? TREATED – 35, 45, 36, 11, 41, 29, 38 NOT TREATED – 10, 18, 8, 29, 17, 8, 11

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