Exhibit 8A 3. Refer to Exhibit 8A. The most likely method to get protein 3 into a solution is by using? O a. 6M HCI O b. NaOH OC. SDS o d. beta merchaptoethanol Oe. centrifugation
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- Mention assays other than biuret and lowry assays that are used to detect the presence of proteins. Talk about the principle, the advantages, and the disadvantages.disadvantage of using protein blastWrite down the factors responsible for the stability of proteins. Mention the major factors only write the heading of thoose factor then explain it.
- 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.present briefly the principle of size exclusion chromatography. give a brief description of the use of protein assays.give two disadvantages to using the biuret reaction to measure protein concentration compared to measuring the protein absorbance directly at 280 nm.
- Analysis of a protein is taking place. The enzymic acivity of this protein is stable up to temperatures of 40 degrees celsius. ph values are between 2.5 and 11.5. Now, size exclusion chromatography is being done. Use the graph below and analytical methods to determine molecular weight of protein.Please 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.Can someone help me answer non-graded bio questions pertaining to lactase I'm trying to understand it more?
- Give two advantages to using the biuret reaction to measure protein concentration compared to measuring the protein absorbance directly at 280 nm.a. State the importance of using following reagents in SDS-PAGE. 1. Acrylamide 2. Bisacrylamide 3. Tetramethylethylelediamine 4. Glycerol 5. Ammonium persulfate b. Briefly describe the importance of two dimensional electrophoresis in protein separation?A protein collected through affinity chromatography displays no activity even though it is found to have a high concentration using the Bradford protein assay. What best explains these findings? A. The Bradford reagent was prepared incorrectly. B. The active site is occupied by free ligand. C. The protein is bound to the column. D. The protein does not catalyze the reaction of interest.