Enzyme A, B, and C having the following properties are to be separated by various chromatography at pH 7.0. Describe the expected outcome with a diagram and detailed description. Enzyme A, Molecular weight 35 kDa, pl=6.6 Enzyme B, Molecular weight 43 kDa, pl=5.4 Enzyme C, Molecular weight 65 kDa, pl=7.4
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- An enzyme (molecular weight= 24 kDa, pI= 5.5) is contaminated with two other proteins, one witha similar molecular mass and a pI of 7.0 while the other has a molecular mass of 100 kDa and a pIof 5.4. Suggest how the contaminated enzyme can be purified.Describe how you would make the following solution containing two enzymes. 1 mL total volume in Buffer X with 10nM of enzyme A and 50nM of enzyme B You are given a solution of enzyme A at 1 mg/mL and a solution of enzyme B at 1 mg/mL. The molecular weight of enzyme A is 75,000 g/mol and the molecular weight of enzyme B is 130,000 g/mol.You have an initial solution in which you added quantities of “A” and “B” such that there is 4.5 M “A” and 2.5 M “B” and no complex (“AB”) at time 0. After equilibrium, you are able to isolate and quantitate the “AB” complex, and find its concentration is 1.5 M. Given that RT is 0.59 kcal/mol, what is the delta Go’ for the association reaction?
- What is the likely keq for an enzyme that has a deltaG =-18.3kj/mol?The formation constants at 25°C for Fe(CN)4-6 and Fe(EDTA)2– are 1.00 x 1037 and 2.10 x 1014, respectively. Answer the questions below. 1) Calculate K under standard conditions for the reaction Fe(EDTA)2−(aq) + 6CN−(aq) ----> Fe(CN)4−6(aq) + EDTA4−(aq) 2) Calculate ΔG° for the reaction. (kJ/mol)A biochemist discovers and purifies a new enzyme, generating the purification table below. Procedure Total Protein (Mg) Activity (Units) Crude Extract 20,000 4,000,000 Precipitation (Salt) 5,000 3,000,000 Precipitation (pH) 4,000 1,000,000 Ion Exchange Chromatography 200 800,000 Affinity Chromatography 50 750,000 Size-exclusion Chromatography 45 675,000 a) From the information given in the table, calculate the specific activity of the enzymeafter each purification procedure.b) Which of the purification procedures used for this enzyme is most effective (i.e., givesthe greatest relative…
- If the average molar mass of a sample of soybean oil is 1500 g/mol, how many grams of NaOH are needed to saponify 5.0 g of the oil?The following table shows the molecular masses (Mr) and isoelectric points (pI) of five proteins: Protein Mr pI Chicken egg white lysozyme 14,000 11.0 Carbonic anhydrase 30,000 5.4 Ovalbumin 45,000 4.5 Phosphorylase b 97,000 6.7 Lactate dehydrogenase 140,000 7.12 (a) A solution containing these five proteins was adjusted to pH 7.0 and then applied to a SIZE-EXCLUSION COLUMN. Assume that these five protein molecules are spherical in shape. Which protein is likely to be eluted LAST from the column? Explain briefly. (b) In another experiment, this protein mixture was first adjusted to pH 6.7 before applying to a CATION-EXCHANGE COLUMN. (i)What is the net charge on phosphorylase b? (ii) Which of these five proteins will bind to the CATION-EXCHANGER? Explain briefly.vWhat is the difference of measuring proteins through UV-VIS spectroscopy at 280 nm and at 595 nm with the presence of the Bradford reagent? (note: explain not less than 5 sentences).
- 1)Ubiquitin is a small protein with a monoisotopic mass of 8560 Da. a) Electrospray ionization of this small protein typically results in major charge states of +8, +9, +10, +11, +12, and +13. Using this information, complete the table below, assuming the charges on each come from protonation. Report mass and m/z values to the ones place. b) Using the data you entered in the table, sketch an expected ESI-MS spectrum for ubiquitin. Label each peak with its charge state. What do you notice about the spacing of peaks along the x-axis. c)The figure shows an experimentally obtained electrospray mass spectrum for ubiquitin. Compare this spectrum to the spectrum you predicted. Are there any differences? If so, what might cause these differences?Given the following choices,a. what is the structure of the product of the reaction catalysed by ACAT?b. structure of the product produced from the reaction catalysed by phospolipase A2?c. general structure of TAGd. structure of glycerolPropanamide and methyl acetate have about the same molar mass, both are quite soluble in water, and yet the boiling point of propanamide is 486 K, whereas that of methyl acetate is 330 K. Explain.