If the absorbance at540nm of a biuret and protein solution containing 0.25mg/ml of protein .24 the absorbance of a biuret and protein and dna solution containing.25mg/ml of protein and 0.5mg/ml dna should be note the total volume is the same in both solutions 0.24 0.72 0.48 not enough infor

If the absorbance at540nm of a biuret and protein solution containing 0.25mg/ml of protein .24 the absorbance of a biuret and protein and dna solution containing.25mg/ml of protein and 0.5mg/ml dna should be note the total volume is the same in both solutions 0.24 0.72 0.48 not enough infor

Name: If the absorbance at540nm of a biuret and protein solution containing
Uploaded: 2024-03-20T06:42:41.000Z
Channel: Bartleby
Description: If the absorbance at540nm of a biuret and protein solution containing 0.25mg/ml of protein .24 the absorbance of a biuret and protein and dna solution containing.25mg/ml of protein and 0.5mg/ml dna should be note the total volume is the same in both

Curren'S Math For Meds: Dosages & Sol

11th Edition

ISBN:9781305143531

Author:CURREN

Publisher:CURREN

Chapter21: Heparin Infusion Calculations

Section: Chapter Questions

Problem 1.3P

See similar textbooks

Similar questions

10 tab of acetaminophen 500 mg molar absorptivity= 14520 @ 243nm. The total weight of the 10tab is 5278 mg. I take a sample equivalent to 100mg of tablet and I diluted it in 100mL, I took an aliquot of 10mL and I diluted it in 250mL, of these I took 25mL and I diluted them in 250mL. Calculate the weight per tablet. Absorbance = 0.944
The protein concentration of a known standard is 100mg/mL If you prepared a serial dilution, mixing 10μL of protein with 40μL of water what would be concentrations of the first 3 dilutions?
To prepare a gel sample, you want to load 50 ng total of protein/well. You have added 200 μL of protein in 800 µL reagent and measured your sample by Bradford A595 to be 0.7 mg/mL - your dilution is unaccounted for at this point. Assuming a total final volume of 20 μL, what volume of protein sample, buffer and 4X SDS PAGE Loading Dye needs to be mixed to create a final sample of 50 ng protein in 20 μL?
Protein Solubility 3.5 5.5 5 5 0.068 0.028 Absorbance 0.098 Conc.(mg/ml) 0.195 0.130 0.044 0.9% 2.786% 9.429% 11.3: % solubility 4.179% The above table indicates the concentration of protein in the diluted supernatant and the supernatant before dilution at different pH. Dilution Factor 30 22.5 15 PH 7.5 1.5 4.5 5 0.027 3 0.042 Protein Solubility Versus pH 6.5 6 4.5 pH Value The above figure shows a plot of protein solubility versus pH. 50 7.5 7.5 50 0.032 0.053 8.5 50 0.054 0.100 21.429% 9 Please provide a brief discussion and explanation of the results. (using isoelectric point and net charge to explain)
Penicillin G potassium 5000 units Isotonic Sodium Chloride Solution ad 15 mL Sig. Nose drop Using soluble penicillin tablets, each containing 100,000 units of crystalline penicillin G potassium, explain how you would obtain penicillin G potassium needed in compounding the prescription.
Protein Solubility 3.5 5 0.028 Absorbance 0.098 Conc.(mg/ml) 0.195 0.044 0.9% 2.786% 9.429% 11.3: % solubility 4.179% The above table indicates the concentration of protein in the diluted supernatant and the supernatant before dilution at different pH. Dilution Factor 30 22.5 pH 15 7.5 1.5 4.5 5 0.027 3 0.042 5.5 5 0.068 0.130 Protein Solubility Versus pH 6 6.5 4.5 pH Value The above figure shows a plot of protein solubility versus pH. 50 Please provide a brief discussion and explanation of the results. 7.5 7.5 50 0.032 0.053 9 8.5 50 0.054 0.100 21.429%
Size Size Crude Anion Cation 2) Exclusion Exclusion Lysate Exchange Exchange 1 2 Total Protein Concentration 15.2 6.6 2 3.75 4.7 (mg/mL) Final Sample Volume 60 30 20 4 3 (mL) Enzyme Specific Activity 0.43 1.7 7.25 18.3 12.5 (units/mgprotein) Based on your protein purification sample data, in which of the purification steps in your protocol did you effectively purify your enzyme? Select all that apply. a) anion exchange correct b) cation exchange correct c) size exclusion 1 correct d) size exclusion 2
5/ n SO a- 6.46 The following data show the binding of Mg2+ ions with a protein containing n equivalent sites: [Mg2+ ] total/μM [Mg2+ ]free/μM 108 Com 35 180 65 288 501 115 248 752 446 Apply the Scatchard plot to determine n and Ka. The protein concentration is 98 µM.
Figure 3: ● ● ● ● ● ● KDa ● 97.4 66.2 45.0 ● 31.0- 21.5 14.4 S-1 p-1 S-2 2-0 This figure was generated by centrifuging a pura sample of protein, removing the supernatant, and resuspending the pellet in the same volume as the supernatant to allow direct comparison. The supernatant and pellet samples were then prepared for SDS-PAGE identically and run via normal SDS-PAGE procedures. In the figure, "s" means supernatant and "p" means pellet. The text or number after the dash represents a different condition. For example, s-1 and p-1 are the supernatant and pellet samples under condition 1. It is not shown, but under wild-type conditions, essentially all of the protein is found in the supernatant. S-3 ● What does the intensity of each band represent? ● Would you find soluble protein in the supernatant or pellet? Why? Would you find aggregated protein in the supernatant or pellet? Why? For each condition (there are 5 different conditions), is there a higher percentage of the total protein…
After three minutes, the concentration of drug Zip in the red blood cells is 10 mmoles l-1. What is the average rate of entry of drug Zip into the red blood cells in units of moles min-1 red blood cell-1 during the first three minutes after placing the red blood cells into the bathing solution? Assume that each red blood cell occupies about 1 x 10-13 liters.
A mixture of proteins contains Pepsinogen (35 kDa), Fumarase (49 kDa), Transferrin (80 kDa) and Thyroglobulin (340 kDa). Rank these proteins based on the order of their elution from a gel filtration column (1 being the first one to elute and 4 as the last one). Throglobulin Pepsinogen Fumarase Transferrin
You need a buff er at pH 7.5 for use in purifying a protein at 4°C. You have chosen Tris, pK 8.08, ΔH° = 50 kJ · mol−1. You carefully make up 0.01 M Tris buffer, pH 7.5 at 25°C, and store it in the cold to equilibrate it to the temperature of the purifi cation. When you measure the pH of the temperature-equilibrated buff er it has increased to 8.1. What is the explanation for this increase? How can you avoid this problem?