The following list of proteins are found in a mixture and are to be separated by 2D gel electrophoresis:Molecular weight (Daltons)ProteinIsoelectric pointMyoglobin17,0007.0Cytochrome C12,00010.6IgG150,0006.4Hemoglobin64,5007.1Insulin5,8005.4Human serum albumin66,0004.6Histone H315,00010.8Рepsin33,0001.0In 2D electrophoresis, the mixture is first subjected to isoelectric focusing, separating them via theirisoelectric pH values (corresponding to the horizontal axis, then subjected to SDS-PAGE to separate viamolecular weight (corresponding to the vertical axis), where large proteins stay at top and smallerproteins go towards the bottom.24pH710direction of electric current150MW (kDa)100ВEA5024pH710With this information, match the letters of the bands to the proper protein based on the data given.Band LetterProteinADE

In 2D gel electrophoresis, is a 2 step-based separation of protein. In the first dimension, the…

Answered: The following list of proteins are…

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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When developing the zymogram using a destaining solution, a researcher observed wedge shaped bands with protein. What could be the possible reason for such an observation?
GenAlex Medical, a leading manufacturer of medical laboratory equipment, is designing a new automated system that can detect normal levels of dissolved immunoglobin A (70. to 312. mg/dL), using a blood sample that is as small as 250 µL. Calculate the minimum mass in milligrams of immunoglobin A that the new system must be able to detect. Be sure your answer has the correct number of significant digits. mg 0 x10 X
What are the sources of error in the Acid Hematin Method? Factors involved in the difference between oxyhemoglobin values and cyanmethemoglobin values in normal individuals.
A student conducted an experiment on protein isolation from mungbean. After isolating the protein, the student characterized the isolate using the Bradford assay. Standard solutions of bovine serum albumin (BSA) were prepared and 0.1 ml of each solution was subjected to Bradford assay. Absorbance readings were made at 595 nm and summarized below. Concentration of Absorbance at BSA (mg/mL) 595 nm 1.2 1.12 1.0 0.97 0.8 0.79 0.6 0.59 0.4 0.37 0.2 0.17 The student found out that 0.1 mL sample of the protein extract from mungbean gave an absorbance of 0.83 in the same assay. 1. How much was the concentration of the protein in the mungbean sample (in mg/mL)? Show all equations and calculations. 2. Draw a graph for the readings of the standard solutions and absorbances. Indicate the approximate location of the calculated concentration of the mungbean sample in your graph.
After the electrophoretic separation, the proteins are transferred to a nitrocellulose membrane prior to staining with antibodies specific for the protein understudy. Describe in detail how the primary and secondary antibodies could aid in the protein detection process.
You have the following reagents available Rat anti-Keratin 8 antibody specific for mouse Keratin 8, Rabbit polyclonal antibody against mouse keratin 5 and antifade reagent with DAPI to stain DNA. Both primary antibodies work best at 1:500 dilution. A) What additional reagents would you need to perform immunostaining of frozen sections of mouse thymus tissue for Keratin 8 that is expressed in cortical thymic epithelial cells and Keratin 5 that is expressed in mouse medullary thymic epithelial cells? B) Create a staining protocol including all tubes and appropriate controls to stain 4 slides with frozen thymic sections. You will need 200ul of antibody staining solution for each slide.
In Western Blots and ELISAS, the following molecules are used:  Tween-20 SDS Goat anti-rabbit IgG (whole molecule) – HRP Rabbit anti-egg albumin Bovine IgG Rabbit anti-bovine IgG – HRP Egg albumin (globular protein – what is Molecular weight?) Milk protein (globular protein – what is Molecular weight?) TMB Beta-mercaptoethanol Methanol HCl May you explain the reasons why they are used?
I understand that microarrays are being used to define the molecular abnormality and the prognosis in some patients with leukaemia. What are microarrays?
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 #:…
Recombinant Protein G from Streptococcus are covalently attached in an oriented fashion to magnetic beads. Bovine Serum is added and the antibodies are captured by the beads. Using the magnetic device, beads are attached and unbound material is washed away. Antibodies are eluted using a lower pH buffer and the solution is neutralized. The equilibration step is adding the serum sample to the buffer-equilibrated (pH 6) magnetic Protein G beads. What was expected to occur if this step was missed? When we mix the samples on the mixer, it was crucial that there was no foam present in the sample - why is this and what part of the mixture would be "foamy" at this step? Lastly, we use an neutralizing buffer after eluting the samples from the column. Why is this step important?
A unique aquatic plant was discovered from a lagoon in El Nido, Palawan. To determine the protein content of the plant, an adequate amount of the plant extract was acquired, and Bradford assay was performed. Determine the total protein concentration, in µg/mL, of the acquired plant extract. A bovine serum albumin (BSA) stock solution with a concentration of 250 µg/mL was used and mixtures with the following compositions and absorbance readings were prepared: Volume of BSA (mL) Volume of water (mL) Absorbance Tube # at 595 nm 1 0.00 2.00 0.000 2 0.20 1.80 0.112 3 0.40 1.60 0.225 4 0.60 1.40 0.318 5 0.80 1.20 0.432 6 1.00 1.00 0.551 The absorbance reading of the plant extract is 0.275.
The figures 1 and 2 show the agarose- gel electrophoresis pattern of the serum proteins of a healthy cow and sheep. Discuss briefly on the components of the serum proteins from these two animals. Albumin a az Fig. 1. Representative agar gel electrophoretic pattern of serum sample from a healthy cow Albumin | Fig. 2. Representative agar gel electrophoretic pattem of serum sample from a healthy sheep

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