1)Which methods can be used for total protein determination? Please explain briefly. 2) Evaluate the total protein determination methods according to their sensitivity. 3) Explain for what purposes the determination of total protein is used.
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1)Which methods can be used for total protein determination? Please explain briefly.
2) Evaluate the total protein determination methods according to their sensitivity.
3) Explain for what purposes the determination of total protein is used.
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- Explain the protein determination methods and when to use which method?What level of RF in serum is clinically significant? Why is a 1:20 dilution of patient serum, rather than undiluted patient serum, used for the qualitative test? Describe how the RF concentration is computed?Please explain the theoretical background (positive color reactions and what is being detected) involved in the different qualitative test for proteins that has been isolated intact or hydrolyzed. Please directly answer the theoretical background (positive color reactions and what is being detected) of each testNITROPRUSSIDE TEST - FOLLIN'S REACTION - SULLIVAN'S TEST - PAULY REACTION - LIEBERMAN'S TEST -
- 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?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.I need to prepare a standard calibration curve for gamma globulin. absorbances on Y and mg of standard protein per assay on X. used 0.1mg/ml gamma stock for tubes 2-6. (Water (ml), gamma (ml), Abosrbance)--> (.036, .004, .290) (.036, .008, .358) (.024, .016, .341) (.016, .024, .520) (.008, .032, .597) - What is the math and how do you get the standard curve?
- Please explain the theoretical background (positive color reactions and what is being detected) involved in the different qualitative test for proteins that has been isolated intact or hydrolyzed. Please directly answer the theoretical background (positive color reactions and what is being detected) of each test GENERAL: BIURET - NINHYDRIN SPECIFIC XANTHOPROTEIC TEST - MILLON'S TEST - HOPKINS-COLE TEST - SAKAGUCHI TEST - LEAD ACETATE TEST - NITROPRUSSIDE TEST - FOLLIN'S REACTION - SULLIVAN'S TEST - PAULY REACTION - LIEBERMAN'S TEST -Identify the most commonly used technique for diagnosing COVID-19? And the clinical sample for each technique?topic: Preparation of a Calibration CurveStandard Bovine Serum Albumin (BSA) solution Why is BSA used as a standard for protein content determination? Can other proteins be usedinstead?
- Which of the following is incorrect about blood glucose test interpretation A) fasting plasma glucose 6.1-6.8 defined as having IGT and should probably be screened again after a year or so. B) 2 results>7mmmol/l defined as having diabetes C) fasting plasma glucose >6mmol, recall for further test. D) fasting or random plasma glucose, on one reading of <11.1mmol/l is diagnostic of diabetesThe accompanying figure is from an electrophoresis experiment using SDS–PAGE. The left lane has the following standards: bovine serum albumin (MW 66,000), ovalbumin (MW45,000), glyceraldehyde 3-phosphate dehydrogenase (MW 36,000),carbonic anhydrase (MW 24,000), and trypsinogen (MW 20,000).The right lane is an unknown. Calculate the MW of the unknown.The correct order of steps when purifying a protein are: Group of answer choices 1)Growing bacterial culture for fusion protein; 2)Harvesting IPTG-induced cultures; 3)Lysing bacterial cell; 4)Removing insoluble debris; 5)Using Affinity Chromatography to purify protein. 1)Growing bacterial culture for fusion protein; 2) Breaking open bacterial cells; 3) Removing insoluble debris: 4) Harvesting IPTG-induced cultures; 5)Using Affinity Chromatography to purify protein 1) Growing bacterial culture for fusion protein; 2) Lysing bacterial cells; 3) Harvesting IPTG-induced cultures; 4) Removing insoluble debris: 5)Purifying protein by affinity chromatography 1)Growing bacterial culture for fusion protein; 2) Removing insoluble debris; 3) Harvesting IPTG-induced cultures; 4)Breaking open bacterial cells; 5)Purifying protein by affinity chromatography