Fundamentals of General, Organic, and Biological Chemistry, Books a la Carte Plus Mastering Chemistry with Pearson eText -- Access Card Package (8th Edition)
8th Edition
ISBN: 9780134261256
Author: John McMurray, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Videos
Textbook Question
Chapter 18.4, Problem 18.1CIAP
The proteins collagen, bovine insulin, and human hemoglobin have isoelectric points of 6.6, 5.4, and 7.1, respectively. Suppose a sample containing these proteins is subjected to electrophoresis in a buffer at pH 6.6. Describe the motion of each with respect to the positive and negative electrodes in the electrophoresis apparatus.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Three dipeptides are separated by electrophoresis at ph 5.8. if the dipeptides are Arg-trp, Asp-thr, and Val-met, describe the motion of each with respect tothe positive and negative electrodes in the electrophoresis apparatus.
Penicillin is hydrolyzed and thereby rendered inactive by penicillinase, an enzyme present in some resistant bacteria. The mass of this enzyme in Staphylococcus aureus is 29.6 kd. The amount of penicillin hydrolyzed in 1 minute in 10 ml solution containing 10–9 g of purified penicillinase was measured as a function of the concentration of penicillin. Assume that the concentration of penicillin does not change during the assay.
[Penicillin] µM Amount hydrolyzed (nanomoles)
1 0.11
3 0.25
5 0.34
10 0.45
30 0.58
50 0.61
a) Plot V0 versus [S] and 1/V0 1/[S]. Does penicillinase appear to obey Michaelis-Menten kinetics?
b) What is the value of KM?
c) What is the value of Vmax?
d) What is the turnover number of penicillinase under these conditions?
The standard curve to determine the
amount of betacyanin is shown
below.
You extracted a red pigment from a
beet disc (the mass of a disc is 2 g)
using 10 ml of 20% ethanol solution.
You measured absorbance of the
solution above the beet disc every
minute for a total time of 20 minutes.
The increase in absorbance was
linear during a period of time from 1
min to 10 min. The absorbance at 10
min was 0.8. Calculate the amount of
betacyanin extracted from 1g of a
beet tissue per minute.
Explain your calculations. You can
use Excel or a calculator.
Chapter 18 Solutions
Fundamentals of General, Organic, and Biological Chemistry, Books a la Carte Plus Mastering Chemistry with Pearson eText -- Access Card Package (8th Edition)
Ch. 18.2 - Prob. 18.1PCh. 18.2 - Prob. 18.2PCh. 18.3 - Prob. 18.3PCh. 18.3 - Examine the ball-and-stick model of valine in the...Ch. 18.3 - Indicate whether each of the following molecules...Ch. 18.3 - Prob. 18.6PCh. 18.3 - Prob. 18.7KCPCh. 18.3 - Prob. 18.8PCh. 18.3 - Prob. 18.9PCh. 18.3 - Prob. 18.10P
Ch. 18.3 - Prob. 18.11PCh. 18.3 - Prob. 18.12PCh. 18.4 - The proteins collagen, bovine insulin, and human...Ch. 18.4 - Prob. 18.2CIAPCh. 18.4 - Prob. 18.13PCh. 18.4 - Prob. 18.14PCh. 18.5 - Valine is an amino acid with a nonpolar side...Ch. 18.5 - Tripeptides are composed of three amino acids...Ch. 18.5 - Prob. 18.17PCh. 18.5 - Identify the amino acids in the following...Ch. 18.5 - Prob. 18.19PCh. 18.5 - Prob. 18.3CIAPCh. 18.5 - Prob. 18.4CIAPCh. 18.5 - Two of the most complete (balanced) proteins...Ch. 18.6 - Prob. 18.6CIAPCh. 18.6 - Prob. 18.7CIAPCh. 18.6 - (a)What atoms are present in a planar unit in a...Ch. 18.6 - Prob. 18.21PCh. 18.6 - Prob. 18.22PCh. 18.7 - Prob. 18.23PCh. 18.7 - Prob. 18.24PCh. 18.7 - Complete the following two sentences with either...Ch. 18.7 - Prob. 18.26KCPCh. 18.8 - Which of the following pairs of amino acids can...Ch. 18.8 - Look at Table 18.3 and identify the type of...Ch. 18.8 - In Figure 18.3, identify the amino acids that have...Ch. 18.8 - Prob. 18.30PCh. 18.9 - Prob. 18.31PCh. 18.10 - Another endoprotease is trypsin. Trypsin...Ch. 18.10 - Prob. 18.33PCh. 18.10 - Prob. 18.8CIAPCh. 18.10 - Prob. 18.9CIAPCh. 18 - Draw the structure of the following amino acids,...Ch. 18 - Prob. 18.35UKCCh. 18 - Prob. 18.36UKCCh. 18 - Prob. 18.37UKCCh. 18 - Prob. 18.38UKCCh. 18 - Threonine has two chiral centers. Draw L-threonine...Ch. 18 - Name four biological functions of proteins in the...Ch. 18 - Prob. 18.41APCh. 18 - Prob. 18.42APCh. 18 - Prob. 18.43APCh. 18 - Prob. 18.44APCh. 18 - Prob. 18.45APCh. 18 - Prob. 18.46APCh. 18 - Prob. 18.47APCh. 18 - Draw leucine and identify any chiral carbon atoms...Ch. 18 - Prob. 18.49APCh. 18 - Prob. 18.50APCh. 18 - Is histidine hydrophilic or hydrophobic? Explain...Ch. 18 - Prob. 18.52APCh. 18 - At neutral pH, which of the following amino acids...Ch. 18 - Prob. 18.54APCh. 18 - Prob. 18.55APCh. 18 - Prob. 18.56APCh. 18 - Prob. 18.57APCh. 18 - Proteins are usually least soluble in water at...Ch. 18 - Prob. 18.59APCh. 18 - Prob. 18.60APCh. 18 - Prob. 18.61APCh. 18 - Prob. 18.62APCh. 18 - Prob. 18.63APCh. 18 - (a)Identify the amino acids present in the peptide...Ch. 18 - Prob. 18.65APCh. 18 - Prob. 18.66APCh. 18 - Prob. 18.67APCh. 18 - Prob. 18.68APCh. 18 - Prob. 18.69APCh. 18 - Prob. 18.70APCh. 18 - Prob. 18.71APCh. 18 - Prob. 18.72APCh. 18 - Prob. 18.73APCh. 18 - Prob. 18.74APCh. 18 - Prob. 18.75APCh. 18 - What kind of bond would you expect between chains...Ch. 18 - Is the bond formed between each pair in Problem...Ch. 18 - Prob. 18.78APCh. 18 - Prob. 18.79APCh. 18 - Prob. 18.80APCh. 18 - Prob. 18.81APCh. 18 - Prob. 18.82APCh. 18 - Prob. 18.83APCh. 18 - Prob. 18.84APCh. 18 - Prob. 18.85APCh. 18 - Prob. 18.86APCh. 18 - Prob. 18.87APCh. 18 - Prob. 18.88APCh. 18 - Give an example of a protein that has quaternary...Ch. 18 - Prob. 18.90APCh. 18 - Prob. 18.91APCh. 18 - Prob. 18.92APCh. 18 - Prob. 18.93APCh. 18 - Prob. 18.94APCh. 18 - Prob. 18.95APCh. 18 - Prob. 18.96APCh. 18 - Prob. 18.97APCh. 18 - Prob. 18.98CPCh. 18 - Prob. 18.99CPCh. 18 - Prob. 18.100CPCh. 18 - Prob. 18.101CPCh. 18 - Prob. 18.102CPCh. 18 - Prob. 18.103CPCh. 18 - Prob. 18.104CPCh. 18 - Prob. 18.105CPCh. 18 - Prob. 18.106CPCh. 18 - Prob. 18.107CPCh. 18 - Prob. 18.108CPCh. 18 - Prob. 18.109GPCh. 18 - Prob. 18.110GPCh. 18 - Prob. 18.111GPCh. 18 - Prob. 18.112GP
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- A flat (not spherical) tissue engineered skin (thickness 2.5 mm) is attached to the bottom of a dish and cultured with cell media atop it (which has an oxygen concentration of 0.15 mol/m3). The diffusivity of oxygen in the skin is 3.4 E-9 m2/s, and according to experiments that you’ve performed, you want to make sure that the concentration of oxygen in the device doesn’t fall below 0.06 mol/m3. (Below that concentration harms the cells.) The rate of oxygen consumption is -5.9 E-17 mol/[cell◦s]. What is the maximum cellularity (in cells/mL, three significant digits) that this tissue engineered skin can support?arrow_forwardSuppose you wish to sediment a sample of spherical protein molecules (molar mass of 98.1 kg/mol and radius 3.40x10-9 m) in a liquid using a centrifuge. The sample is placed 5.0 cm from the centrifuge's axis of rotation and is rotated at 6000 Hz. a) What is the centripetal acceleration (i.e. the "g") the sample experiences from the centrifuge? b) If the liquid has a density of 900 kg/m3 and the terminal velocity of the protein is 4.10x10 6 m/s, what is the viscosity of the liquid?arrow_forwardA purified protein sample was used in a reaction, resulting in an activity of 696.7 nmol min-1. The reaction volume was 145.0 µL and the final volume before loading the plate was 1,050 µL. The total reaction time was 4.25 min. The amount of protein used in the reaction was 4.270 µg. Calculate the specific activity of the sample (in nmol min-1 µg-1).arrow_forward
- Consider the fluorescence spectra for bovine serum albumin (BSA) below. One solution contains phosphate buffered saline (PBS), while the other contains 1M HCL. Why does the fluorescence change the way it does? I.e., why do we observe a higher peak and a shift to the left under the presence of acid?arrow_forwardA mixture of lipids containing phosphatidic acid, cholesterol, testosterone, and phosphatidylcholine was applied to a hydrophobic interaction chromatography column. The column was washed with a high salt buffer and the lipids were eluted with decreasing salt concentrations. In what order would the lipids be eluted from the column? Explain your answer.arrow_forwardFour proteins Cytochrome C (pI=10.2) Myoglobin (pI=7.2), Hemoglobin (pI = 6.8) and Serum Albumin (pI= 4.8) were used in our gel electrophoresis lab exercise. If the electrophoretic separation is carried out at pH 7.0, which protein would move toward the negative electrode? Cytochrome C Myoglobin Hemoglobinarrow_forward
- Phosphate buffered saline (PBS) is a very common reagent in cell biology labs that do cell culture since is it osmotically stable for most eukaryotic cells. It is often prepared as 10X PBS (10.5 mM KH2PO4, 1.552 M NaCl, 29.7 mM Na2HPO4) to save on shelf space. How would you prepare 1 L of 10X PBS given 1M KH2PO4, NaCl (FW 58.44), 906mM Na2HPO4? What is the concentration of each component in 1X PBS? How would you prepare 750 ml of 1X PBS?arrow_forwardThe α-amylase (α-AM) enzyme secreted by Aspergillus has an isoelectric point of approximately 4.2. If the purification method in problem 1 operates at pH 6.5, would the protein carry a positive charge, negative charge, or net zero charge?arrow_forwardA colleague has successfully purified the enzyme sphingomyelinase from bovine brain. She provides you with the following incomplete purification table: Specific Activity (nmol/min) (nmol/min/mg) (%) Purification Factor (-fold) Total Total Purification Step Activity Yield Protein (mg) 100 1 Whole homogenate 40-60% (NH4);SO4 CM-sepharose ConA-sepharose Gel filtration Isoelectric focusing 88,625 5,685 925 544 51,700 32,067 29,500 31,680 1,855 420 5 0.03 (A) (B) (C) Per your colleague's request, you agree to calculate: (A) the final specific activity, (B) the final % yield, and (C) the final fold-purification. - x x x x *xx x xarrow_forward
- You perform a Bradford assay to determine the concentration of isolated α-lactalbumin. You use 50 μL of a two-fold diluted solution of α-lactalbumin in the assay. You generate a standard curve with the following equation for the line: y = 0.163x + 0.082. The absorbance of your sample was 0.674 AU. What is the concentration of α-lactalbumin, in mg/mL, in your sample? Give your answer to three significant figures.arrow_forwarda Mixtureof the following amino acids is subjected to paper electrophoresis: Gly, Arg and Asp.Which of these amino acids will at (a) pH 2.0 and (b) pH 10 move to the Anode (+) and which will move to the cathode(-)? Motivate your answer.arrow_forwardWhat is the water potential (Ψ) of a 0.2 M sucrose solution in an open water bath at 20 °C?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. Freeman
Lehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON
GCSE Chemistry - Acids and Bases #34; Author: Cognito;https://www.youtube.com/watch?v=vt8fB3MFzLk;License: Standard youtube license