Which protein standard curve would you use to read off the protein concentration of an unknown sample with an absorbancy value of 1.105 1.75 1.50 1.00 0.75 0.50 -O- BSA BGG 0.25 0.00 500 1,000 1,500 2,000 Protein Concentration (pg/ml) Download image. BSA standard curve BGG standard curve Either BSA or BGG standard curves Net Absorbance (595 nm) 25
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- QUESTION 2 You obtained the following raw data when setting up a Bradford standard curve: Absorbancy BSA (mg/ml) 595nm 0.225 0.310 2 0.420 0.510 4 0.610 0.720 0.810 0.915 0.950 9 0.980 10 0.990 After blanking against a bradford-dH20 sample, the protein concentration of an unknown sample was determined using the same method and an absorbancy of 0.583 was obtained. Set up a standard curve, excluding outliers (experimental and statistical) and determine the protein concentration in the unknown sample in mg / ml (up to 3 significant figures).Figure 3: ● ● ● ● ● ● KDa ● 97.4 66.2 45.0 ● 31.0- 21.5 14.4 S-1 p-1 S-2 2-0 This figure was generated by centrifuging a pura sample of protein, removing the supernatant, and resuspending the pellet in the same volume as the supernatant to allow direct comparison. The supernatant and pellet samples were then prepared for SDS-PAGE identically and run via normal SDS-PAGE procedures. In the figure, "s" means supernatant and "p" means pellet. The text or number after the dash represents a different condition. For example, s-1 and p-1 are the supernatant and pellet samples under condition 1. It is not shown, but under wild-type conditions, essentially all of the protein is found in the supernatant. S-3 ● What does the intensity of each band represent? ● Would you find soluble protein in the supernatant or pellet? Why? Would you find aggregated protein in the supernatant or pellet? Why? For each condition (there are 5 different conditions), is there a higher percentage of the total protein…QUESTION 2 You obtained the following raw data when setting up a Biuret standard curve: Absorbancy BSA (mg/ml) 540nm 0.158 1 0.210 2 0.260 0.305 4 0.360 0.410 0.455 7 0.510 8 0.530 9. 0.550 10 0.554 After blanking against a biuret-dH20 sample, the protein concentration of an unknown sample was determined using the same method and an absorbancy of 0.324 was obtained. curve, excluding outliers (experimental and statistical) and determine the protein concentration in the unknown sample in mg / Set up a standard ml (up to 3 significant figures). 5
- QUESTION 2 You obtained the following raw data when setting up a Bradford standard curve: 0 1 2 3 4 BSA (mg/ml) 595nm Absorbancy 6 7 8 9 10 0.225 0.310 0.420 0.510 0.610 0.720 0.810 0.915 0.950 0.980 0.990 After blanking against a bradford-dH₂O sample, the protein concentration of an unknown sample was determined using the same method and an absorbancy of 0.568 was obtained. Set up a standard curve, excluding outliers (experimental and statistical) and determine the protein concentration in the unknown sample in mg/ml (up to 3 significant figures).Question 1 We have received a specialized blood sera that contains antibodies. We want to test whether the antibody will bind to a target on our cell culture. The company that harvested the material has reported that the harvest works best at a 1:250 dilution. What volume of blood sera should we add to make a total volume of 1ml of antibody containing culture media? You may give your answer in any unit you like, but remember to include the unit. Edit Format Table 12pt v Paragraph vQuestion 33 Orciprenaline (C₁₁H₁7NO3, 211.258 g/mol) is a bronchodilator used in the treatment of asthma. The BP assay for orciprenaline tablets is described below. HO The following information was obtained during the assay: Weight of 20 tablets = 2.5564 g Weight of tablet powder assayed = 0.5266 g Absorbance reading - 0.5868 Stated content per tablet = 20 mg A (1%, 1 cm) at 276 nm = 72.3 OH H N OH "Weigh and powder 20 tablets. Shake a quantity of the powder containing 80 mg of orciprenaline sulphate with 50 mL of 0.01 M hydrochloric acid (HCI), filter and add sufficient 0.01 M HCI to the filtrate to produce 100 mL. Dilute 10 mL to 100 mL with 0.01 M HCI and measure the absorbance of the resulting solution at the maximum at 276 nm." Orciprenaline 4 Answer the following questions, explaining your reasoning clearly. a) Calculate the amount of orciprenaline in the tablet powder analyzed. b) Calculate the average amount of orciprenaline per tablet. c) Calculate the percentage of the stated…
- QUESTION 3 The concentration of an unknown protein sample was determined as 2.3 mg/ml. Calculate the concentration of the unknown protein in mM (millimolar) if: Average molecular mass of an amino acid = 118 g/mol The protein is 101 amino acids in length.After three minutes, the concentration of drug Zip in the red blood cells is 10 mmoles l-1. What is the average rate of entry of drug Zip into the red blood cells in units of moles min-1 red blood cell-1 during the first three minutes after placing the red blood cells into the bathing solution? Assume that each red blood cell occupies about 1 x 10-13 liters.Question 1. Viscosity, gelation, and texturing are related to: a. The surface of the protein Or b. Protein wettability c. Protein dispersibility d. Hydrodynamic properties of the protein Question 2: The meat proteins have been classified into three groups according to their biological function and their solubility. These are: I. Contractile or myofibrillar proteins. II. Sarcoplasmic or soluble proteins III. Insoluble or stoma proteins IV. Absorption proteins V. Legume proteins a. I, ll and Ill b. I, IV and V c. I, IV and V d. II, III and V
- QUESTION 4 Which of the following amino acids would stick to a CM-sepharose column at pH 7.07 Choose all that apply. Partial credit is allowed for each correct answer, arnd negative scores are allowed for incorrect answers. O Arginine (pl -10.76) O Glutamic acid (pl 3.22) O Cysteine (pl 5.07) O Histidine (pl 7.59)QUESTION 3 An unknown protein was determined using the following method: Bradford method Reagents Stock Bradford reagent: Dissolve 100 mg Coomassie Brilliant Blue G250 in a mixture consisting of 100ml of 85% phosphoric acid, 50ml of 95% ethanol and 50ml 1M NaOH. Store at 4°C until precipitation occurs, at which point it is discarded. Working Bradford reagent: Prepare fresh by diluting 10ml of stock Bradford reagent to 250ml with distilled water. Stock bovine serum albumin (BSA) solution (10mg/ml): Dissolve 0.2g BSA in 20ml distilled water. Working BSA concentration range: 0.5 – 1.25 mg/ml Method 1. Prepare the following test tubes: Table 1: Preparation of test tubes for the Bradford method Blank Tube 1 Tube 2 Tube 3 Tube 4 Tube 5 Unknown Distilled H20 1.0 ml 0.9ml 0.9ml 0.9ml 0.9ml 0.9ml 0.8ml 0.25 mg/ml BSA 0.1 ml 0.5 mg/ml BSA 0.1 ml 0.75 mg/ml BSA 0.1 ml 1.0 mg/ml BSA 0.1 ml 1.25 mg/ml BSA 0.1ml Unknown 0.2ml protein Working 4.0ml 4.0ml 4.0ml 4.0ml 4.0ml 4.0ml 4.0ml Bradford 2.…Question 28 : In a SDS-PAGE analysis (Indicate the right answer) : A- The proteins are denatured and positively charged by the addition of SDS. B- Large proteins run faster than small proteins. C- If the pHi of a protein corresponds to the pH of the running buffer the protein becomes positively charged (+) and cannot migrate anymore into the gel. D- For reducing disulfide bridges one needs to add a reducing agent such as 2-mercaptoethanol or DTT. E- All is wrong.