In this lab we employed various assays utilizing a biuret reagent‚ coomassie brilliant blue reagent‚ and ultraviolet light in order to determine the identity of six unknown solutions and the concentration of a bovine serum albumin sample. We were given three samples that lacked protein‚ and three samples containing proteins‚ and using a spectrophotometer we assessed the amount of light absorbed versus the light transmitted‚ based on the principles of the Beer-Lambert Law. The three proteins used included
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Bita Heydari Lab report 3 The Effects of Differentiation on Enzymatic Activity Introduction HL-60 cells are capable of undergoing differentiation to induce different cell types. HL-60 cells can undergo morphological changes‚ changes in gene expression‚ and changes in protein synthesis. In the past weeks‚ we were able to conclude that HL-60 cells treated with DMSO and HL-60 cells treated with PMA will differentiate into granulocytes and monocytes upon treatment (1). We were also able to observe
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To purify the protein in the cell lysate from lab 1 through nickel affinity chromatography. Protein purification should result in only one type of protein ideally‚ which is the protein of interest‚ wt-DHFR and mut-DHFR in this case. A pure protein allows for further analysis on the protein to be conducted‚ such as its concentration (Bradford assay)‚ its molecular weight‚ and its biological activity. 2. Overview of experiments Buffer Preparation Add the liquid sodium phosphate‚ solid sodium chloride
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see looking at the Total Protein column on Table 3‚ the most effective step with regard to the percent of remaining protein removed was affinity chromatography because it was able to remove 98.6% of the remaining proteins. In comparison to 81.93% removed during the 65% ammonium sulfate precipitation and 81.3% during the size exclusion. This means that the affinity chromatography removed a big percentage of contaminating proteins. However‚ removing this huge amount of protein left us with a small amount
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If pH > pI‚ then the protein will have a negative charge and if pH < pI‚ the protein will have a positive charge. Buffer I has a pH >5‚ meaning both proteins carry a negative charge and bind to the DEAE (a positively charged resin). (b) pH = pKa + log10(Base/Acid) [Base = mM of sodium acetate; Acid = mM of acetic acid] = 4.7 + log10 (40/40) = 4.7 In order for the catalase to elute from the column‚ it must have lost its negative charge and stopped binding to the DEAE. Lowering the pH
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Task 1 • Describe the structure of an enzyme as a protein‚ in terms of tertiary/ quaternary structures. 1) Primary Structure This is in reference to the order of way that amino acids are connected to form a protein. These are built up from 20 amino acids‚ and follow these structures o A carbon (the alpha carbon) bonded to the four groups below: o A hydrogen atom (H) o A Carboxyl group (-COOH) o An Amino group (-NH2) o A "variable" group or "R" group 2) Secondary Structure This is in reference
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CODE: BIOL 2365 Comparative Biochemistry TITLE: Proteins and Amino Acids RESULTS: Table 1: The results of experiment 1; the Lowry Test Volume of Standard Protein/ Unknown (mL) Absorbance at 750 nm 0 0.000 0.1 0.017 0.3 0.135 0.3 0.155 0.5 0.230 0.7 0.323 0.7 0.310 1.0 0.457 1.0 Unknown 1a 0.463 1.0 Unknown 1b 0.433 1.0 Unknown 2a 0.237 1.0 Unknown 2b 0.159 Table 2: The results of Experiment 2; Ninhydrin Test Amino acid Color X Bright yellow Y Dark yellow
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Protein in the Digestive System Taylor Adams Biol 112- 501 18 April 2016 Introduction Proteins are found in nearly all foods that we eat. Once the food we eat makes its way to our stomachs‚ pepsinogen is released from chief cells. This enzyme mixes with hydrochloric acid in the stomach and begins to break down the proteins. Along with the stomach‚ the small intestine is also an important location for protein breakdown. The proteins from both locations are broken down into amino
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Expressing and Purifying the Recombinant form of Green Fluorescent Protein (rGFP) from the E.coli strain using Ni2+ agarose affinity chromatography technology Abstract The purpose of this experiment was to express and purify the his6-tagged recombinant form of GFP (rGFP) from the organism E.coli using Ni2+ agarose affinity chromatography. The expression of rGFP was confirmed qualitatively using the UV light and was expressed in the E.coli strain BL21 (DE3) (-- removed HTML --) (-- removed HTML
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Purpose: To use a set of standardized procedures to test for simple sugars and starch‚ proteins‚ and fats. Hypotheses: A.) B.) C.) Equipment: -Safety goggles -Lab apron -400 mL beaker -Utility stand with ring clamp -Hot plate -Thermometer -10 mL graduated cylinder -Test-tube racks -8 to 16 test tubes -Test tube holder -Medicine dropper -Rubber stoppers -Test-tube brush -Wax pencil -Distilled water
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