Prescott's Microbiology
11th Edition
ISBN: 9781260211887
Author: WILLEY, Sandman, Wood
Publisher: McGraw Hill
expand_more
expand_more
format_list_bulleted
Question
Chapter 20.3, Problem 2CC
Summary Introduction
Microorganisms generating methane as a
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Theoretical Data
Following the modified protocol for the isolation of Escherichia coli bacteriophage of Encabo (2018)
presented below, compute for the pfu/ml of the chloroform-treated lysate.
1ml
1ml
1ml 1ml
1
Chloroform-treated lysate
1ml
Dilution
10-3
10-4
10-5
0 0 0 0 0
9ml
9ml 9ml
10-1
10-²
10-3
Empty sterile
tubes
Incubate inside ref for 15-20min
+ 0.1 ml lysate-E.coli mix
0.1 ml
9ml 9ml
104
10.5
//
0.1 ml
0.1 ml
+0.5 ml E. coli
↓↓↓↓↓↓
Incubate O/N at 35°C,
observe for plaques
Molten soft agar
overlay
B. Quantification of the Infective E. coli other Bacteriophage Particles in the Raw Sewage
Sample
Volume of Stock Plated (in ml)
Bottom agar
No. of Plaque-Forming Units (pfu)
Ave.
A
B
254
265
132
110
11
23
Please help me answer and explain these questions:
1. Compare the abundance of A280 chromophores (W, Y, and C) to Bradford sites (loosely R and K) in BSA.
2. We used a protocol that corrects the path length in each well and normalizes the absorbance to the value that would be obtained if the path length were 1 cm (the standard path length). Using this observation and your A280 calibration data, what is your measured e280, for BSA?
The purification of cytochrome C begins with 1) yeast homogenization using a bead beater in the presence of BME (a reducing agent) and a protease inhibitor from approximately 900 grams of Baker’s yeast. Then, 2) insoluble cell contents were removed by centrifugation at 4,000 x g for approximately ten minutes. The ruptured cells (lysate) after centrifugation had a total volume of 0 mL and a 1.0 mL aliquot was set aside for further analysis. The following data was obtained from the 1.0 mL aliquot to quantify the protein amount and purity:
The absorbance at 410 nm of the aliquot was 0.460 (1 cm pathlength).
The absorbance at 595 nm from a 1.0 mL Bradford Assay solution that was diluted by 250-fold from the aliquot was 0.681 (1 cm pathlength).
Using the information given,
Calculate the total protein amount in mg from the absorbance at 595 nm.
Calculate the cytochrome C amount in mg from the absorbance at 410 nm using Beer’s Law.
Chapter 20 Solutions
Prescott's Microbiology
Ch. 20.1 - MICRO INQUIRY Given that the DC/HB pathway uses...Ch. 20.1 - Prob. 2MICh. 20.1 - Prob. 1CCCh. 20.1 - Why do methanogens use the reductive acetyl-CoA...Ch. 20.1 - Prob. 3CCCh. 20.1 - Compare the ATP and NADH yield of each of the...Ch. 20.2 - MICRO INQUIRY Identify the potential electron...Ch. 20.2 - Retrieve, Infer, Apply What are thermoacidophiles...Ch. 20.2 - Prob. 2CCCh. 20.2 - Compare the carbon and sulfur metabolism of...
Ch. 20.2 - Prob. 4CCCh. 20.2 - Prob. 5CCCh. 20.3 - MICRO INQUIRY What are the mechanisms by which...Ch. 20.3 - Retrieve, Infer, Apply Why are the growth yields...Ch. 20.3 - Prob. 2CCCh. 20.3 - What is the ecological and practical importance of...Ch. 20.3 - Where are extreme halophiles found, and what is...Ch. 20.3 - What is the difference between sensory rhodopsin...Ch. 20.3 - How is Thermoplasma able to live in acidic, very...Ch. 20.3 - In what way are members of the genus Archaeoglobus...Ch. 20 - Prob. 1RCCh. 20 - Prob. 2RCCh. 20 - Prob. 3RCCh. 20 - Prob. 4RCCh. 20 - Prob. 5RCCh. 20 - Prob. 6RCCh. 20 - Prob. 7RCCh. 20 - Some believe that archaea should not be separate...Ch. 20 - Prob. 2ALCh. 20 - Prob. 3ALCh. 20 - Prob. 4ALCh. 20 - Prob. 5ALCh. 20 - Prob. 6ALCh. 20 - Prob. 7AL
Knowledge Booster
Similar questions
- pls explain Increasing the saturation of the ammonium sulfate is a prerequisite in isolating a target protein that is rich in Cys and Tyr residues. Which of the following techniques should be considered in accurately quantifying the isolated protein?I. Running the isolated protein in a dialysis or GFC set up.II. Using Biuret or BCA assay as the colorimetric quantitation method.III. Using Bradford or Lowry assay as the colorimetric quantitation method.A. I onlyB. II onlyC. I and IIID. I, II and III. Bradford Assay is most suitable to use when the extraction buffer is below the target protein’s pI. This is so because the protein would be morea. Positively charged allowing the CBB G-250 dye to bind via its sulfonate groups.b. Negatively charged allowing the CBB G-250 dye to bind via its sulfonate groups.c. Neutrally charged allowing the CBB G-250 dye to bind via its sulfonate groups.d. Zwitterionic allowing the CBB G-250 dye to bind via its sulfonate groups.arrow_forwardneed help to calculate P1 for amino acid Tryptophan. Also please check if I draw the mechanism correctly and completely???arrow_forwardWhat is the expected yield for plasma membranes isolated by sucrose gradient centrifugation from mouse tissues?arrow_forward
- Q1: What is the significance of a large positive ΔG between a substrate and its ES complex and a small ΔG? Q2: What is the significance of a large negative ΔG between a substrate and its Products compared to a small ΔG?arrow_forwardQuantitatively describe the unique focusing capability of IEF and identify factors that increase resolution of proteins in IEF.arrow_forwardDescribe the bioreactor design consideration to be taken in account during the bioprocessing of animal cell culture. Please discuss which factors influence the choice of bioreactor design?arrow_forward
- Describe the molecular mechanism by which quorumsensing controls bioluminescence in V. fischeri.arrow_forwardhow are SDS-PAGE and BN-PAGE techniques used determine the composition of protein-photosynthetic complexes? also how do they work? please be thorough in the explanation!arrow_forwardSolve: EER= 354- [6.91*24]+ 1.27 * [(9.36*41.8)+(726*1.5748)] = ? Do calculations in the paranthesis first then the bracketsarrow_forward
- The purpose of the progress curve is to determine if an enzymatic reaction rate remains constant for given concentrations of enzyme and substrate, for a given assay time (20 min). How long did the rate of reaction of WGAP remain constant in your experiments? How do you know? What would cause the reaction rate to not be constant and plateau after some time?arrow_forwardWe considered the effects of many parameters in designing bioreactors. Please answer the following questions regarding bubbles in airlift fermenters. Bulleted lists are okay. (a) Why was it undesirable to use a very large bubble size (Diameter >7 mm)? (b) Why was it undesirable to use a very small bubble size (Diameter <7 mm)? (c) Other than varying bubble size, what can be done to further decrease cell death due to entrainment?arrow_forward11) Using the data above, construct Lineweaver-Burk plots. First, graph the inverse of the reaction velocity (rate of reaction) data in column II versus the inverse of the methanol concentration in column I. Then, on the same graph, plot the inverse of the reaction velocity (rate of reaction) data in column III versus the inverse of the methanol concentration in column Iarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning