Help please Table 1. Purification of rat liver histidase.Purification stepProteinTotal activitySpecific activitynmol/min per mgPurification-foldYieldmgnmol/minHomogenateHeating at 65 °CAmmonium sulfatefractionation (0)DEAE-Sephadex columnAmmonium sulfatefractionation (II)QAE-Sephadex column17,718.13,097.7503.812,138.08,751.18.335.80.6852.816.510072246871926.92,156.71,730.930.064.3441894140.23279.5342.7500.30.65Rev Invest Clin 2004; Vol. 56(1):43-50; Producción de histidasa recombinante de higado de rata; Victor Ortiz, Nimbre Torres, Armando R Tovar.A) In the table above, what columns provide evidence that the purity of the protein is increasing with eachprotein purification step?B) There is always a trade-off. As the purity of a protein INCREASES, what factors DECREASE?C) Based on your answer to part B, above, what is the ultimate limiting factor to the level of purity of a protein?

We purify and isolate a specific protein from a crude extract or homogenate using several…

Table 1. Purification of rat liver histidase. Purification step Homogenate Heating at 65 °C Ammonium sulfate fractionation (1) DEAE-Sephadex column Ammonium sulfate fractionation (II) QAE-Sephadex column Protein mg 17,718.1 3,097.7 503.8 71.9 26.9 0.232 Total activity nmol/min 12,138.0 8,751.1 8.335.8 2,156.7 1,730.9 79.5 Specific activity nmol/min per mg 0.685 2.8 16.5 30.0 64.3 342.7 Purification -fold 1 4 24 44 94 500.3 Yield % 100 72 68 18 14 0.65 Rev Invest Clin 2004; Vol. 56(1):43-50; Producción de histidasa recombinante de hígado de rata; Victor Ortiz, Nimbre Torres, Armando R. Tovar. A) In the table above, what columns provide evidence that the purity of the protein is increasing with each protein purification step? B) There is always a trade-off. As the purity of a protein INCREASES, what factors DECREASE? C) Based on your answer to part B, above, what is the ultimate limiting factor to the level of purity of a protein?

Table 1. Purification of rat liver histidase. Purification step Homogenate Heating at 65 °C Ammonium sulfate fractionation (1) DEAE-Sephadex column Ammonium sulfate fractionation (II) QAE-Sephadex column Protein mg 17,718.1 3,097.7 503.8 71.9 26.9 0.232 Total activity nmol/min 12,138.0 8,751.1 8.335.8 2,156.7 1,730.9 79.5 Specific activity nmol/min per mg 0.685 2.8 16.5 30.0 64.3 342.7 Purification -fold 1 4 24 44 94 500.3 Yield % 100 72 68 18 14 0.65 Rev Invest Clin 2004; Vol. 56(1):43-50; Producción de histidasa recombinante de hígado de rata; Victor Ortiz, Nimbre Torres, Armando R. Tovar. A) In the table above, what columns provide evidence that the purity of the protein is increasing with each protein purification step? B) There is always a trade-off. As the purity of a protein INCREASES, what factors DECREASE? C) Based on your answer to part B, above, what is the ultimate limiting factor to the level of purity of a protein?

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter10: From Proteins To Phenotypes

Section: Chapter Questions

Problem 9QP: a. Compounds A, B, C, and D are known to be intermediates in the pathway for production of protein...

See similar textbooks

Similar questions

Chitinase is a protein that breaks down chitin, a primary component of the cell wall in fungi, scales in fish and exoskeletons of arthropods. The activity of chitinase extracted from a plant was shown to be optimum at pH 5. You were tasked to prepare 300 mL of 150 mM buffer solution for further analysis of the extracted chitinase. REAGENTS Ka 2.5M Acetic acid Solid NaOAc•3H2O [136.08g/mol] 1.76 x 10-5 2.5M NH3 Solid NH4Cl [53.49g/mol] 5.6 x 10-10 2.5M Lactic acid Solid sodium lactate [112.06g/mol] 4.0 x 10-5 5 M HCl 5M NaOH Pls show sol'ns 1. Given the following reagents, give the moles of each component (acid & base).2. What are the mass/volume of the components needed to prepare the buffer? 3. What will the pH of the buffer be if 1mL of 5 M NaOH was added?
The transport of aspirin (pKa = 3.5, structure shown here) from the digestive tract to the circulation occurs by nonmediated absorption into cells lining the stomach (where pH = 0.8) and the small intestine (where pH 6.0). Do you expect absorption to be faster in the stomach or in the small intestine?
A tetrapeptide, glutamate-glycine-alanine-lysine, is prepared at at concentration of 1 mM (0.001 M) and is measured in the standard setup (pathlength of 1 cm). What is the approximate absorbance of this peptide at 280 nm? Hint: if the peptide contained a single tryptophan, the answer would be about 10. 10 280 1 0
a protein collected through affinity chromatography displays no activity even though it is found to have a high concentration using the bradford protein essay. what best explains these findings?
What is the fractional occupancy of a protein binding site when the ligand concentration (L) =1mM and the ligand equilibrium binding constant at the binding site K10= 10microM. 0.01 B.0.1 C.0.91 D.0.99 none of the listed values
An experiment was carried out to measure the reaction rate of hydrolysis of acetylcholme (substrate) with serum enzymes (Eadie, 1949). In the experiment, two experiments were conducted, namely experiment 1 without using a prostigmine inhibitor and experiment 2 using a prostigmine inhibitor at 1.5 x 10^-7 mol/l. the data obtained are: a. Is prostigmine competitive or noncompetitive inhibitor? b. determine the value of km and rmax for the two experiments, compare
EGTA (ethylene glycol-bis(β-amino ethyl ether)-N,N,N′,N′-tetraacetic acid) is a chelating agent with high affinity and specificity for Ca2+. By microinjecting acell with an appropriate Ca2+-EGTA solution, an experimenter can prevent cytosolic [Ca2+] from rising above 10+7 M. How would EGTA microinjection affect a cell’s response to vasopressin ? To glucagon?
3 i. Define Biological Value (BV) of Proteinsii. What are the advantages of this protein evaluation method when compared to Nbalance and chemical score?5iii. A bull consumes 7 kg DM of feed containing 60 g N/kg. The bull excretes 120 g N inthe faeces and 50 g N in the urine. The feacal and urinary N had 20 g metabolic feacalnitrogen (MFN) and 6 g endogenous urinary nitrogen (EUN) respectively.Calculate the BV of the protein in the diet.
Give the general Adiar equation for the binding of a ligand to a dimeric protein. Explain further what your understanding is of the terms "no-, positive-, and negative cooperativity” and graphically present the relationship between Ȳ and [S] for each of these cases. Also, give the relationship between the constants Kb1 and Kb2 in each case.
The ESI-MS spectrum in positive ionization mode for lysozyme is obtained. a. What is the molecular weight of the protein to 5 significant figures based on the two highlighted ion species? b. What is the charge of the peaks at 1101.5 and 1789.2.
THOUGHT QUESTION Imagine we identify a gene that is directly responsible for the effects of vasopressin on male mammals, including humans-we will call it trust1-that leads to the production of a vasopressin receptor in the brain, which we will call TRUST1. There are different versions of trust1, all of which lead to different levels of the behavior associated with this neuropeptide on male behavior. Give some examples where it would be a good idea to know a particular males genotype-that is, which of the trust1 genes he has. Give an example of when you think science has gone too far and this information should not be known.
Amino acids are not stored in the body. Describe how excess amino acids are processed in the cell.