I. Data A. Solubility in water Sample alanine glutamic acid arginine albumin B. Color Reactions of Amino Acids 1. Ninhydrin Test Color of Ninhydrin solution: Sample alanine glycine glutamic acid tyrosine albumin Experiment No. 2 AMINO ACIDS AND PROTEINS Solubility (Soluble, Partially Soluble, Insoluble) Color original solution Color with red litmus paper Color with blue litmus paper Color with Ninhydrin Is the solution acidic, basic, or neutral? Color after 10 min.
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Experiment
AMINO ACIDS AND PROTEINS
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- 1. List down the amino acids in the following format Amino Acid Physiological Significance 3 letter Code 1 letter code Chemical Structure 2. List down the different qualitative and quantitative tests for Amino Acids Test Reagents Principle Positive Reaction/ResultLaboratory Activity- Assignment (Color Reaction of Proteins) 1. Provide the Principles and detailed procedures of the following tests for the "Color Reaction of Proteins". D. Ninhydrin Test E. Hopkins-Cole Test F. Sulfur Test G. Heller's TestCOLOR REACTION OF PROTEINS Question Guide: 1. Write the positive result, the chemical group responsible for the positive and the importance of each test. Test Positive Result Chemical Group Biuret Ninhydrin Xanthoprotei Millon's Hopkins-Cole Lead Acetate Pauly Bromine Water Sakaguchi
- C. Choosing the Proper Buffer Solution 1. Choosing the Proper Buffer Solution In Protein Precipitation, two liters of 5mM buffer solution with pH 5.2 is needed in the isolation of albumin. Which among the following buffer solution is best fitted for said purpose? Justify your answer. Buffer solutions pKa Acetate buffer 4.73 Tris- (hydroxymethy) aminomethane 8.08 Phosphate buffer 7.20 Discussion: 2. Preparation of the Chosen Buffer System Calculate and measure the amounts (in grams if solid and in mL if liquid) of weak acid and conjugate base needed to be able to prepare the chosen buffer system in part A above. Express your answer in useful units (that is, prepare it from practical amounts or concentrations of starting materials). D. Titration of an Amino acid Graph: titration of Glutamic acid Glu Glu Glu" Glu- COOH Co0 co0 Co0 H,N*-C -H H,N-C-H H,N*-c-H H,N -C -H CH2 CH2 CH, CH2 CH CH, CH, CH2 COOH соон co0 Co0 14 12 10 pK pH pkg Isoelectric point pk, 1.0 2.0 3.0 Equivalents of COH"…. A prescriber ordered 240 mL of ¾ strength Sustacal PO B.I.D. Explain how you would use water as a diluent to mix this solution. Show your work with units and describe how much water and how much Sustacal you would use to create this mixture..MATCHING TYPE; Match A to B A. Acrolein tesT Benedicts test Biuret test Iodine test Barfoed’s test Molisch test Seliwanoff’s test Fehling’s test Salkowski’s test Furter-Meyer test B. A. The test for the presence of cholesterol. B. The test for reducing sugars in acidic solution. C. The test is used to detect cholesterol in a solution D. The test for the presence of starch/amylose. E. The test for presence of reducing sugars in alkali solution. F. The general test for carbohydrates. G. This method is used to detect the presence of tocopherols H. The test to distinguish monosaccharides from disaccharides I. The test for the presence of fats or glycerin. J. The test to determine ketohexose from an aldohexose.
- The reults for the macroscopic part: 0.30M glycerin – solution was translucent (could see text behind the test tube) 0.15M NaCl – solution was opaque (could not see text behind the test tube) 0.30M NaCl – solution was opaque (could not see text behind the test tube) 0.15M glucose – solution was translucent (could see text behind the test tube) 0.30M glucose – solution was opaque (could not see text behind the test tube) 0.30M Urea – solution was translucent (could see text behind the test tube) Results for microscopic part: 0.30M glycerin – no cells present 0.15M NaCl – normal sized cells 0.30M NaCl – crenated (shrunken and star-shaped) cells 0.15M glucose – no cells present 0.30M glucose – normal sized cells 0.30M Urea – no cells present Determine the osmolarity (hypoosmotic, isosmotic, or hyperosmotic) and tonicity (hypotonic, isotonic, hypertonic) of the following solutions.In which solutions did the osmolarity NOT match the tonicity? For those solutions, why did the osmolarity…Example of a Protein Purification Scheme: Purification of the Enzyme Xanthine Dehydrogenase from a Fungus Volume Total Total Specific Percent Fraction (mL) Protein (mg) Activity Activity Recovery 1. Crude extract 2. Salt precipitate 3. Ion-exchange chromatography |4. Molecular-sieve chromatography 5. Immunoaffinity chromatography 3,800 22,800 2,460 0.108 100 165 2,800 1,190 0.425 48 65 100 720 7.2 29 40 14.5 23 1.8 275 152.108 11 Calculate the specific activity of step#4. Note that percent recovery=% Yield.. Discuss the properties of potassium iodide solution, and how it results in the detection of starch. . Explain the meaning of each color that results in Starch Test, such as: 11.1 Yellow to brown and; 11.2 Blue to black.
- Choose among proteins A, B, C, and D. 1. Protein that will most strongly bind to an anion exchange colum. 2. Protein that will elute last in gel filtration chromatography. 3. Protein that will elute first in hydrophobic interaction chromatography. 4. Protein that will elute last in a carbohydrate containing colum.1&1/2 tsp po BID x 14 days #QS How many milliliters should the pharmacy dispense?Absorbance of urea for a diabetic patient is 0.335 while 0.214 is the absorbance of standard kit for the same test, calculate the concentration of this test ? Concentration of standard kit = 50 mg/dl. Repl...