Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Question
Chapter 8, Problem 26P
Interpretation Introduction
Interpretation:
The reason corresponding to the fact that
Concept introduction:
A constant which expresses the substrate’s concentration if the velocity of reaction equals to the half of the maximum velocity of the reaction is known as Michaelis-Menten constant. It is denoted by
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Choice and Preparation of a Buffer System1. Choosing the proper buffer solution
In Protein Precipitation, two liters of 5mM buffer solution with pH 5.2 is needed in the isolation of albumin. Which among the following buffer solution is best fitted for said purpose? Justify your answer.Buffer solutions pKa Acetate buffer 4.73Tris- (hydroxymethy) aminomethane 8.08Phosphate buffer 7.20
2. Preparation of the chosen buffer system
Calculate and measure the amounts (in grams if solid and in mL if liquid) of weak acid and conjugate base needed to be able to prepare the chosen buffer system in part A above. Express your answer in useful units (that is, prepare it from practical amounts or concentrations of starting materials).
200 ml of a 2% protein solution containing an enzyme that you want to purify. Half of the sample is subjected to method A, consisting of fractionated precipitations and 5 ml of final solution are obtained, with a concentration protein equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml, with protein richness equal to 10 mg / ml and with an activity enzymatic also equal to 2000 U / ml. You want to know: a) Which of the two methods has provided the purest enzyme. b) By which of the methods the greatest amount of enzyme has been obtained.
Quantitative Estimation of Amino Acids by Ninhydrin
http://vlab.amrita.edu/?sub=3&brch=63&sim=156&cnt=2
can u help me with question 2 of the assignment questions
Based on the experimental data provided, estimate the amount of amino acid in the given unknown solution by Ninhydrin method.
SI No.
Volume of standard amino acid solution (ml)
Amount of amino acid (µg)
OD at 570nm
1
Blank
0
2
0.2
0.12
3
0.4
0.25
4
0.6
0.45
5
0.8
0.55
6
1.0
100
0.68
7
Unknown (0.5ml)
0.41
Chapter 8 Solutions
Biochemistry
Ch. 8 - Prob. 1PCh. 8 - Prob. 2PCh. 8 - Prob. 3PCh. 8 - Prob. 4PCh. 8 - Prob. 5PCh. 8 - Prob. 6PCh. 8 - Prob. 7PCh. 8 - Prob. 8PCh. 8 - Prob. 9PCh. 8 - Prob. 10P
Ch. 8 - Prob. 11PCh. 8 - Prob. 12PCh. 8 - Prob. 13PCh. 8 - Prob. 14PCh. 8 - Prob. 15PCh. 8 - Prob. 16PCh. 8 - Prob. 17PCh. 8 - Prob. 18PCh. 8 - Prob. 19PCh. 8 - Prob. 20PCh. 8 - Prob. 21PCh. 8 - Prob. 22PCh. 8 - Prob. 23PCh. 8 - Prob. 24PCh. 8 - Prob. 25PCh. 8 - Prob. 26PCh. 8 - Prob. 27PCh. 8 - Prob. 28PCh. 8 - Prob. 29PCh. 8 - Prob. 30PCh. 8 - Prob. 31PCh. 8 - Prob. 32PCh. 8 - Prob. 33PCh. 8 - Prob. 34PCh. 8 - Prob. 35PCh. 8 - Prob. 36PCh. 8 - Prob. 37PCh. 8 - Prob. 38PCh. 8 - Prob. 39PCh. 8 - Prob. 40PCh. 8 - Prob. 41PCh. 8 - Prob. 42PCh. 8 - Prob. 43PCh. 8 - Prob. 44PCh. 8 - Prob. 45PCh. 8 - Prob. 46PCh. 8 - Prob. 47PCh. 8 - Prob. 48PCh. 8 - Prob. 49P
Knowledge Booster
Similar questions
- Many biochemists go bananas, and justifiably, when they see a Michaelis-Menten plot like the one shown here. Vmax ол [S] To better understand their outrage, calculate V as a fraction of Vmax when [S] = 10 Kè and [S] = 20 KM. M When [S] = 10 KM, Vo = 0.91 Vmax When [S] = 20 KM, Vo = 95 Incorrect Vmax.arrow_forwardBiochemical Reactions Using good details, compare and contrast the pairs of different biochemical reactions. Create your own comparing and contrasting map similar to the one below to show your understanding. Anabolism Catabolism First Pair of Describe Describe differences here différences here Reaction Types Describe similarities here Second Describe Pair of differences here Reaction Types Describe similarties here Describe differences here Pair of Reaction Describe sampar lus heru Types Describe Par of 110 Describe differences here Describe différences here Describe differences herearrow_forwardI2 An immobilized enzyme plug flow reactor (PFR) contains a very porous honeycomb structure that has an enzyme immobilized on its surface. The substrate (S) enters the reactor at a concentration of 0.05 mole L-1along with an uncompetitive inhibitor (I) with a concentration of 0.01 mole L-1. The enzyme properties are such that: Vmax= 1.2 x 10-8mole cm-2sec-1, Km= 0.12 mole L-1. For the inhibitor KI= 0.05 mole L-1. The flowrate through the reactor is such that kL= 10-4cm sec-1. The surface area to volume ratio of the honeycomb structure in the bioreactor is 1 cm-1. Estimate the residence time needed to achieve a 90 % conversion of the substrate. If the flowrate through the reactor is 100 L hr-1, what is the total volume (L) of the reactor needed to achieve this conversion? If the L/D ratio of the reactor is 10, what are the dimensions (ft) of the reactor? Repeat these calculations if external mass transfer effects are ignored.arrow_forward
- 1 pt pt 9146 Bb 9146 Bb 1031 Class Etsy E Traps E Traps New Free Chat + ☆ 出口 keAssignment/takeCovalentActivity.do?locator-assignment-take [References] You do an enzyme kinetic experiment and calculate a Vmax of 118 μmol per minute. If each assay used 0.10 mL of an enzyme solution that had a concentration of 0.20 mg/mL, what would be the turnover number if the enzyme had a molecular weight of 128,000 g/mol? (Enter your answer to two significant figures.) turnover number = sec-1 D 1 pt Submit Answer Try Another Version 2 item attempts remaining estion stion 5 on 6 7 1pt 1 pt 1 pt 1pt 1pt 1pt 1 pt 1 pt D is the substrate concentration multiplied by the catalytic constant. KM is equivalent to the substrate concentration multiplied by the ratio of rate constants for the formation and dissociation of the enzyme-substrate complex. KM is equivalent to the substrate concentration. KM is equivalent to the substrate concentration divided by 2 A: KM is equivalent to the substrate concentration…arrow_forwardPołymer formation from a pool of available monomers with a range of chemical functionalities contributes to biochemical molecular complexity. True Falsearrow_forwardChemistry I'm thinking DEAE makes the most sense but I want a second opinion. I'm also not sure how to elute the protein. I'll rate with a good answer, thanks!arrow_forward
- Enzyme X exhibits maximum activity at pH- 6.3. X shows a fairly sharp decrease in its activity when the pH goes much lower than 5.8. One likely interpretation of this pH activity is that: a Glu residue on the enzyme is involved in the reaction. O the enzyme uses NADH has a cofactor the enzyme uses coenzyme A has a cofactor O a Tyr residue on the enzyme is involved in the reaction. O a His residue on the enzyme is involved in the reactionarrow_forwardMore ratios. Through the use of nuclear magnetic resonance spectroscopy, it is possible to determine the ratio between the protonated and deprotonated forms of buffers. (a) Suppose the ratio of [ A- ]A I to [HA] is determined to be 0.1 for a buffer with pKar6.0.pKa = 6.0. What is the pH? (b) For a different buffer, 91974 suppose the ratio of [ A- ]lA J to [HA] is determined to be 0.1 and the pHpH is 7.0. In this case, what is the pKapKa of the buffer? (c) For another buffer with pKa=7.5PKa = 7.5 at pH 8.0pH 8.0, what is the expected ratio of [ A- ][A ] to [HA]? doarrow_forwardI need help with understanding this homework problem. Please answer it clearly and explain why. This is specifically for Biochemistry.arrow_forward
- Protein,nfolded Proteinţolded Under certain conditions, a specific protein has the following thermodynamic parameters for going from the unfolded state to the folded state: AH = – 300 kJ/mol, and TAS = – 400 kJ/mol. Under those conditions, the equilibrium would lie more toward neither would predominate - the fraction of total protein that's folded would = fraction unfolded. the folded state the unfolded state O It is impossible to predict the position of the equilibrium from AH and TAS.arrow_forward1. You need 0.5 liter of a 0.1 M buffer for a biochemical reaction that you plan to perform at pH 2.0. On the shelf in your laboratory you have available phosphoric acid, and the amino acids aspartate, glycine, glutamate, tyrosine, and histidine (all you have available are the fully deprotonated forms of the molecules); these are the only buffer materials you have available. (The pKa values for these compounds are given below.) For phosphoric acid, pKal1 = 2.12, pKa2 = 7.21, and pKa3 = 12.32 For aspartate, pKaCOOH = 1.88, pKaNH3+ = 9.60, pKa sidechain = 3.65 For glycine, pKaCOOH = 2.34, pKaNH3+ = 9.60 For glutamate, pKaCOOH = 2.19, pKaNH3+ = 9.67, pKa sidechain = 4.25 For histidine, pKɑCOOH = 1.82, pKɑNH3+ = 9.17, pKa sidechain = 6.00 For tyrosine, pKaCOOH = 2.20, pKaNH3+ = 9.11, pKa sidechain = 10.07 a. Of these possible buffers, which is likely to yield the greatest resistance to pH change from the starting pH of 2.0, assuming that you were going to run a biochemical reaction that…arrow_forwardmultiple choice, choose the correct answer You stumble upon a potential inhibitor (I) for HIV protease, so you now have to perform a few experiments to characterize its behaviour. You find that if you add an excess of substrate to the reaction in the presence of inhibitor, enzyme activity increases but to only 0.5 Vmax to that observed in the absence of inhibitor. The affinity of the substrate for the enzyme is unaffected by the inhibitor. If you treated the enzyme with inhibitor, then dialyse the protein into a buffer solution without inhibitor, the activity is restored. What type of inhibitor is I?1. Uncompetitive2. Competitive3. Non-competitive 4. Irreversiblearrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning