You run 5 standard proteins listed below on a size-exclusion (gel filtration) column with limit of200,000Da. Please draw a chromatogram on a separate page with each peak and both axeslabeled.ProteinB-AmylaseAlcohol dehydrogenaseBovine albuminCarbonic anhydraseCytochomeA280MW223,8000.582,0000.666,463 0.4530,000 0.4312,0000.8

Size-exclusion chromatography is a separation technique where the proteins are separated based on…

Answered: You run 5 standard proteins listed…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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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 #:…
Human serum albumin is another protein that has an extremely long half life in the body. Due to this, the low probability event, glycation does take place. Write a rate law for this reaction: Rate = k[glucose] Rate = k[hemoglobin] Rate = k [glucose hemoglobin albumin]
o NB4: Why do you think you first had to make the 1 mM solution instead of working directly from the stock solution?
Consider the proteins in the table below. Protein Isoelectric point (pl) М.W. Alcohol dehydrogenase 150,000 5.5 Cytochrome C 12,400 10.5 Serum albumin 66,000 5.3 B-Amylase 200,000 5.7 Apoferitin 443,000 4.0 Fill in the blank. If the mixture of proteins above was subjected to anion exchange chromatography at pH 8, from the column. would be the first protein to elute
The dialysis bag membrane in the figure is permeable to water and to the simple sugars only. The final solute concentration will: • Stay same without change • Reach equilibrium on both sides. • Sucrose concentration will be higher inside the bag. "Environment" 0.01 M sucrose 0.01 M glucose "Cell" • Glucose concentration will be higher inside the bag. 0.03 M sucrose 0.02 M glucose 0,01 M fructose • Fructose concentration will be higher inside the bag.
We want to measure the activity of alanine aminotransferase (ALAT) present in a serum. The reaction catalyzed by the enzyme is: Reaction 1: I- *H₂N- glutamate H - C-COO CH₂ CH₂ COO 0.1 M phosphate buffer pH 7.4 : 550 μL 1.2 M alanine: 100 μL CH3 pyruvate CH3 C time (min) A340 CIO O COO The enzyme reaction is alized in the following conditions: In a 1 cm-cuvette are added: COO™ pyruvate lactate dehydrogenase* (LDH, 300 µμg.mL-¹): 50 μL 1.5 mM NADH : 200 μL 0.04 M a-ketoglutarate: 500 µL serum containing ALAT: 600 μµL ALAT NADH + H+ 0 0.915 a-cétoglutarate COO LDH * Lactate dehydrogenase (LDH) reduces pyruvate into lactate, with the concomitant oxydation of NADH. This allows to indirectly measure the amount of product formed. с=0 CH₂ 1 0.741 Reaction 2: NAD+ CH₂ COO™ H-C CH3 OH COO™ lactate alanine H + *H3N-C The reaction is performed at 25 °C and the absorbance at 340 nm is monitored every minute, for 5 min. The absorbance values are given in the table below: Data: ENADH at 340 nm =…
the 2 answers for both questions are right are right i just need the steps, i gave you 2 questions so you can double check your that the steps are right
Select the product for the following cyclization CHO OH OH OH H OH OH Но HO HO OH но Но - OH HO HO Но. OH H- OH OH H H H ČH2OH 1 3 О 1&2 1 2
d/e/1FAIpQLSfTle9UfP15_VUqFI-ACEQd1XBykXv5Lr4dEMQbLJ1d6fCupw/viewform Students subjected three samples of five different molecules to gel electrophoresis as shown in Figure 1 A B C DE +2 3 Wells 4 8. Which of the following statements best explains the pattern seen on the * gel with regard to the size and charge of molecules A and B? 1 point molecules A and B are positively charged, and molecule A is smaller than molecule B. molecules A and B are positively charged, and molecule A is larger than molecule B. molecules A and B are negatively charged, and molecule A is smaller than molecule B. molecules A and B are negatively charged, and molecule A is larger than molecule B. Sign out
Which of the following options shows the correct order of fastest to slowest motion of chloride ions, glycine and proteins through the separating gel? Chloride ions > Proteins > Glycine Glycine > Chloride ions > Proteins Chloride ions > Glycine > Protein Protein > Chloride ions > Glycine
I am not understanding why TA of alcohol precipitation is used as TA of purified protein. I provided 2 photos, 1 with the questions and the correct answer, and the other photo is a screenshot of the explanation.
Please type answer not write by hend

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