Abstract The objective of this lab was to measure the amount of protein from a piece of beef liver . This was done by taking the liver‚ blending it and then using a centrifuge to separate the supernatant from the pellet. Once that was completed‚ ammonium sulfate was added to the supernatant‚ chilled and then spun for a second time. Next‚ 20 mL of water is added to the pellet‚ stirred and the volume was recorded. The teacher calculated the total mass of liver to be 10.098g. Lastly a spectronic
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concentrations were done by using y = mx+b. The equation used for BCA was y = .0011x +.2019. The value y represents the absorbance reading for the unknown value. When plugged into the equation x was solved for the concentration of unknown samples of BSA. The concentration for unknowns 1‚2‚ and 3 using the BCA method were 524‚ 2332‚ 32 µg/mL. In graph 4 the standards were recorded using the Bradford method and produced a linear line and out of the line produced‚ a linear regression equation of y =
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that we can use to test the absorbency. We placed the distilled water and chicken samples into small tubes that could be placed in the spectrophotometer in order to get the absorbency reading. We got the readings and recorded the data in order to determine whether our hypothesis was supported. MATERIALS and METHODS: We adjusted the wavelength on the spectrophotometer to A595 (Lab instructions). We blanked the machine using a tube
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Expression and Purification of Human Platelet-Derived Growth Factor Beta (PDGF-B) Rachel C. Hermina-Stewart* and Elsie I. Parés-Matos† *Industrial Biotechnology Program‚ †Department of Chemistry University of Puerto Rico-Mayagüez Campus rachel.hermina@upr.edu December 14‚ 2009 ABSTRACT. Platelet-Derived Growth Factor (PDGF) is one of many proteins that regulate cellular growth and division. The PDGF family consists mainly of five different isoforms called as PDGF-A‚ PDGF-B‚ PDGF-C and PDGF-D. Three
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Q 1. In this practical exercise you will be using biuret reagent. Why is biuret reagent used in this practical? The biuret reagent is used to assess the concentration of the protein because peptide bonds occur with the same frequency per amino acid in the peptide. The intensity of the colour‚ and therefore the absorption‚ is directly proportional to the protein concentration. Q 2. What is the experimental reason for constructing a standard curve? Multiple samples with known properties
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An Le Foundation Biology lab BRADFORD PROTEIN DISCUSSION ESSAY The appearance of blue color showed the present of protein in the BSA dilutions. The more diluted the solution was‚ the less blue it was. The R2 value of the standard curve of BSA dilution was obtained to be 0.9972‚ which is close to 1. The closer to 1 the R2 value was‚ the more accurate the linear portion was. The error percentage of each unknown was large: 25.9% for skim milk‚ 95% for soy sauce‚ and 64.7% for egg white. The vast
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concentration beer lambert law is not applied because of the electrostatic interactions between molecules and at high concentration‚ there are changes in refractive index. Spectrophotometer: -A spectrophotometer is an instrument that measures the intensity of light absorbed after it passes through a sample solution. With the spectrophotometer‚ the amount of a known chemical substance (concentrations) can be known by measuring the intensity of light detected. It is used in quantitative analysis in various
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A protein standard curve was generated by using the protein standard (1 ampule) measurement at 595 nm. Standard curve was prepared as shown in Table 4. Bovine serum albumin (BSA) was diluted with distilled water. The absorbance of each sample were measured using spectrophotometer at 595nm. Standard protein curve was plotted according to the concentration of protein where the x-axis and y-axis represent protein standard concentration and absorbance (595 nm) respectively. 3.10.2 Protein Determination
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divalent Mg2+ ions for activity‚ and can catalyse the hydrolysis of PNPP to p-nitrophenol (PNP) and inorganic phosphate (see prac 1 schedule). Remember that PNP is yellow at alkaline pH‚ and its appearance can be detected at 405 nm using a spectrophotometer. Because this enzyme works best at alkali pH‚ we do not need to use a timepoint-quench method (as we did with Acid P)‚ but can monitor the ΔA 405 directly in real
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blot method was used to detect the molecular weight of proteins which is selected for three different antibodies: α-β-actin targeting the α and β isoforms of actin protein‚ α-GADPH targeting Glyceraldehyde 3-phosphate dehydrogenase‚ (GAPDH); and α-BSA which targets bovine liver protein. Target protein was identified with TANDEM mass spectrometry. The experiment can be labeled a success since it fulfilled its primary goal of isolation and identification of protein and also provided an appropriate
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