In what order would the following proteins eluted from a gel filtration column of Sephadex G200: Myoglobin(Mr= 16,000), catalase (Mr-500,000), cytochrome c (Mr-12,000), chymotrypsinogen (Mr=26,000), and hemoglobin (Mr-66,000)? Explain your answer
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- In the ESTIMATION OF TOTAL SERUM CHOLESTEROL using ZAK AND HENLY’S METHOD, explain why should the serum stay clear? What are the implications of using a turbid serum sample?Total protein: Do you think that refractive index could be used as a regular method for serum protein determinations? If yes, what limitations does it have. If not, why not? What are the major interferences in the biuret method? Refractometry method?Which fractions measured from your gel filtration experiment had the most and least amount of protein detected? Which fraction likely contained the most myoglobin based off molecular weight and protein presence? Which fraction likely contained the most egg albumin based off molecular weight and protein presence? Which samples measured from your ion exchange experiment had the most protein detected? Calculate the approximate pI of your proteins using the ion exchange Table 2. Ion Exchange Samples Tested by Bradford Assay Concentration BSA (μg/mL) Concentration BSA (mg/mL) Volume of Sample added to Bradford Reagent (μL) Absorbance at 595 nm Standard 1 250 0.25 50 0.32 Standard 2 125 0.125 50 0.16 Standard 3 62.5 0.0625 50 0.08 Standard 4 31.25 0.03125 50 0.04 Standard 5 15.625 0.015625 50 0.02 Blank 0.00 0.00 0.00 Table 3. Gel Filtration Fractions Tested by Bradford Assay Fraction #:…
- In a mixture of five proteins listed, draw an elution profile (Absorbance vs. mL eluted, arbitrary) for the purification of the listed proteins on a gel filtration chromatography resin: cytochrome c (pI = 5.4; Mr = 13,000), immunoglobulin G (pI = 7.3; Mr = 145,000), ribonuclease A (pI = 9.6; Mr = 13,700), RNA polymerase (pI = 6.3; Mr = 450,000), human serum albumin (pI = 5.4; Mr = 68,500). Label your elution peaks. Draw a sketch of an SDS-PAGE, reflecting the mobility of the above mixture as they elute from the column. Label you protein bands.If a protein lysate obtained is 1003 ug/ml What would be the total concentration of each lysate that is loaded into their well if you load just 25 ul of each?Approximate nH for each protein from its Hill plot. Which proteins exhibits a greater degree of positive cooperativity, normal hemoglobin or the mutant hemoglobin?
- 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.What does an A280 of 0.000 indicate? What does this reading indicate in the context of your column chromatography? Are there still proteins adhering to the column? Do you know anything about the proteins which are still adhering to the column?When pure hemoglobin (molecular mass of 64,000 Da) is separated by the following methods, what major molecular mass species do you expect to see? Gel filtration chromotography: Gel filtration with 6M Urea: SDS-PAGE with DDT: SDS-PAGE:
- In the experiment performed for the determination of cholesterol, the function of the calibration curve obtained using 25-400mg/dL standard cholesterol solutions was determined as y= 0.0009x. If the absorbance of the serum sample is determined as 0.28, what is the amount of cholesterol in the sample, in mg/L?A gel filtration column with a fractionation range of 1.5-20 kDa is used to separate out the proteins shown below. If these proteins are collected into separate fractions in between the void volume and total volume, in which order will they elute? Indicate if any of the proteins are found in the void volume or total volume fractions. Protein Z - 3330Da Protein Y - 13kDa Protein X - 1.3kDa I. Total volume fraction II. Third protein fraction III. Second protein fraction IV. First protein fraction V. Void volume fractionA gel filtration column was calibrated by measuring elution volumes for two proteins of known mass: glutamate dehydrogenase, 290 kDa with elution volume 20.8 mL; serum albumin, 37 kDa with elution volume 42.5 mL Use these values to determine the equation of the straight line graph that relates log molar mass to elution volume. The elution volume of an unknown protein was 32.2 mL. Use the equation just determined above to estimate the molar mass of the protein in kDa units. Don't round your answer until the end to ensure your answer is within the accepted range. Round your answer to the nearest whole number (e.g. If you calculated 27.52, input your answer as 28).