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- True or false? the size of the pores of a polyavrymide gel decrease as the concentration of polyacrylamide increases. SDS is a detergent that partially denatures proteins.Predict the number of bands and apparent mol. wt. of the following proteins on SDS gels. 1. Immunoglobulin G in a reducing gel (β-mercaptoethanol added in the sample solution) – the light chains have a molecular weight of 25,000 Da and the heavy chains 50,000 Da.Advantages and disadvantages of the following dosage forms:○ Suspension○ Parenteral Solutions○ Creams○ Pastes○ Sprays
- Part a. You making 30 mo of agarose gel. Sybersafe A concentration 1000x. How much you will add......ul to the gel. b. You will be loading 20 your diagnostic digest onto your gal. The loading dye you have been provided is 5x concentrated. You will add..... ? ul to your sample before loading your gel.F. How much of a 100 mg/mL stock of Ampicillin would you need to add to 400 mL for a 100 ug/mL final concentration? What fold stock is this?[protein] volume [protein] [protein] in to Sample Lysate in "gel- load 5 in 20 protein in Name volume assay* lysate ready" ul sample protein 3.9 2 µl Hg/ml Tilapia 19.9 10 μι Hg/ml 18.2 2 µl Hg/ml Cod >20 14 10 μι Hg/ml 9.4 15 2 µl ug/ml Sole >20 6. 10 μι ug/ml > >
- Use correct sig figs The concentration of a purified monoclonal antibody was measured using UV280 nm. The sample was diluted (200 μL of purified antibody in 800 μL buffer) prior to analysis using a spectrophotometer. Calculate the concentration of antibody in the purified fraction if the Abs=0.95 of the diluted antibody. The molar absorptivity is known to be 191,411.6 M-1cm-1 and the molecular weight is 150 kDa. The pathlength for the cuvette is 1 cm.Please asap. thankyou. The following diagram represents the results of hemoglobin samples of 5 patients (1-5) that were run on an electrophoresis gel at pH 9.2. The first 3 lanes show the control samples, for comparison. Using only the letters "AA" "AS" and "SS", fill in the blanks below indicating the most likely genotype of each patient, based on these protein electrophoresis results. The following diagram represents the results of hemoglobin samples of 5 patients (1-5) that were run on an electrophoresis gel at pH 9.2. The first 3 lanes show the control samples, for comparison. Using only the letters "AA" "AS" and "SS", fill in the blanks below indicating the most likely genotype of each patient, based on these protein electrophoresis results. Patient 1 Patient 2 Patient 3 Patient 4 Patient 5True or False. Write T if the statement is true, F if false 1. Blood smears made from EDTA specimens must be prepared within 3 hours of collection to preserve the integrity of the blood cells.2. A specimen collected and placed in an evacuated tube with a gel barrier may prevent blood glycolysis for up to 24 hours.3. Specimens that require separation of the serum or plasma from the cells should be centrifuged within 1 hour of arrival in the lab.4. Serum specimens can be centrifuged right away as opposed to plasma specimens that needs standing for at least 30 minutes before allowed to be centrifuged,5. Removal of the cap/stopper of the evacuated tube before centrifugation allows loss of carbon dioxide and a decrease in the blood specimen pH.
- 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"…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…Give me a clear Detailed Solution..no need handwritten