Search for the principles and the uses of the following methods for protein measurements and provide an image that will serve as your visual reference. Serum Protein Electrophoresis Isoelectric Focusing Ion Exchange Chromatography Turbidimetry Solvent Fractionation
Q: Various methods have been developed for detecting proteins. Describe how radioisotopes and…
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Q: Given that the normal range for serum protein is about 7 g/100ml and albumin is about 4 g/100ml,…
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Q: what type of gel must be used when the protein size is 2500 Da
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Q: Using 25 μL of serum, how much diluent would be needed to create a 1:2 dilution? ______ μL
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Q: In isoelectric focusing, a protein sample is applied at the end of a gel with an immobilized pH…
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Q: Total Protein Determination Spectroscopy Values CREATE CALIBRATION CURVE? DRAWN CONCENTRATION AND…
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Q: Describe the principles involved in protein purification by affinity chromatography. Be thorough
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Q: Discuss the functions and components of Biuret dye in protein content determination.
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Search for the principles and the uses of the following methods for protein measurements and provide an image that will serve as your visual reference.
- Serum Protein Electrophoresis
- Isoelectric Focusing
- Ion Exchange Chromatography
- Turbidimetry
- Solvent Fractionation
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- Compare and contrast the following protein characterization techniques in terms of the principles governing their functions. size exclusion chromatography vs ion-exchange chromatographyCompare and contrast the following protein characterization techniques in terms of the principles governing their functions Gel filtration chromatography and isoelectric precipitationTotal 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?
- Total Protein Determination Spectroscopy Values CREATE CALIBRATION CURVE? DRAWN CONCENTRATION AND ABSORPTION CURVEPlease explain!!! select all that are right the same Protein X was purified from tissue source A and tissue source B, yielding the following results: Protein X, sample A: specific activity = 100 U/mg; fold-purification = 200 Protein X, sample B: specific activity = 1000 U/mg; fold-purification = 100 Which of the following statements are correct? a) Protein X, sample A has a higher level of purity than Protein X, sample B. b) Protein X, sample B has a higher level of purity than Protein X, sample A. c) Tissue source A has a higher specific activity for Protein X than tissue source B. d) Tissue source B has a higher specific activity for Protein X than tissue source A.Sketch the appearance after visualization of a protein mixture containing the seven proteins (fibrinogen, y-globulin, collagen, ovalbumin, myoglobin, hemoglobin, insulin) when subjected to two-dimensional (2D) gel electrophoresis.
- Various methods have been developed for detecting proteins. Describe how radioisotopes and autoradiography can be used for labeling and detecting proteins. How does Western blotting detect proteins?Immunofluorescence and Fluorescent livecell imaging techniques can both be used to determine protein localisation.List the advantages and disadvantages of using immunofluorescence andfluorescent live cell imagingWhat is the basis for the separation of proteins by the following techniques? (a) gel-filtration chromatography(b) affinity chromatography(c) ion-exchange chromatography
- 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: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 fractionFrom this standard curve and chart below, does the separation of molecules in the mixture appear successful from the gel filtration? Is there a clearlydefined separation between molecules? Explain your conclusions. Parameters required for calculation of coefficient (Kd) for unknown protein Volume eluted (mL) Which variable does this volume represent in the equation for Kd? Fraction with maximal DNP-Aspartate detected 36 Vt Fraction with maximal Protein detected 24 Ve Fraction with maximal Blue dextran detected 6 Vo