biological compatibility with a dicarboxylate pseudo crown receptor designed to satisfy the size and charge requirements of the Pb2+ cation. Spectroscopic measurements with LF1 were performed under simulated physiological conditions (20 mM HEPES‚ buffer pH 7). LF1 displays a characteristic fluorescein-like absorption band in the visible region centred at 490 nm and weak fluorescence. Upon addition of Pb2+‚ the fluorescence intensity intensity of LF1 increases by 18 fold with the absorption and emission
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| Buffer A | Buffer B | Mass of NaC2H3O2 used to prepare buffer (grams) | | | Volume of buffer prepared (mL) | 100.0 | 100.0 | Molar concentration of HC2H3O2 in buffer (M) | 0.1 | 1.0 | Initial pH of buffer | | | Volume of 0.5 M NaOH to raise pH by 2 units (mL) | | | Volume of 0.5 M HCl to lower pH by 2 units (mL) | | | Volume of 0.5 M NaOH at equivalence point (mL) | | | Data Analysis 1. Write reaction equations to explain how your acetic acid-acetate buffer reacts
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and non-buffered solutions and then monitoring the pH changes as a strong acid or base was added to the solution. By performing this experiment‚ it was found that with increasing amounts of buffer in the prepared solutions there was better resistance against pH changes. This was because the strong acid or base was converted to it’s weak conjugate. The solution with little or no buffer had no resistance to pH changes. The Irresistible
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First‚ the pH probes were calibrated using buffer solutions with known pH values of 4.01 ± 0.01 and 7.00 ± 0.01. First‚ the pH probes were placed in the 4.01 buffer and the probe was calibrated‚ then rinsed with distilled water‚ placed into the 7.00 buffer‚ and calibrated again. The pH probe was very close in its measurements‚ as the 4.01 ± 0.01 buffer was measured to have a pH of 4.01 ± 0.01‚ and the 7.00 ± 0.01 buffer was measured to have a pH of 6.87 ± 0.01. After the calibration
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performed to precipitate out LDH and other proteins. Components such as nucleic acids and sugars‚ which are more soluble‚ remained in the supernatant. In this step 0.13g of ammonium sulfate salt was slowly added per each ml of the 40% supernatant as the solution was stirring. Enzyme assay and protein assay were performed. The results indicated 4600±100 unit enzyme activity concentration and 75±2 mg of protein in the 60% pellet (Raw Data tables 1-A‚2). The enzyme assay was performed on the 60% sup as well
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LEE ET AL.: JOURNAL OF AOAC INTERNATIONAL VOL. 88‚ NO. 5‚ 2005 1269 DIETARY SUPPLEMENTS Determination of Total Monomeric Anthocyanin Pigment Content of Fruit Juices‚ Beverages‚ Natural Colorants‚ and Wines by the pH Differential Method: Collaborative Study JUNGMIN LEE U.S. Department of Agriculture‚ Agricultural Research Service‚ Pacific West Area (PWA)‚ Horticultural Crops Research Laboratory Worksite‚ 29603 University of Idaho Ln‚ Parma‚ ID 83660 ROBERT W. DURST and RONALD E. WROLSTAD Oregon
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[Accessed 22 Oct. 2014]. Inkling.com‚ (2014). Inkling. [online] Available at: https://www.inkling.com/read/marks-medical-biochemistry-lieberman-marks-4th/chapter-45/i--plasma-proteins-maintain [Accessed 13 Oct. 2014]. Media.lanecc.edu‚ (2014). Chemical Buffer Systems and Acid-Base Balance. [online] Available at: http://media.lanecc.edu/users/driscolln/RT127/Softchalk/Acid_Base_Lesson/Acid_Base_Lesson4.html [Accessed 13 Oct. 2014]. Research.vet.upenn.edu‚ (2014). Milk Urea Nitrogen. [online] Available at:
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tubes 2 .Test tube rack 3. Small Para film squares 4. Distilled water 5. Potato extract 6. Catechol 7. Phenylthiourea 8. Disposable gloves 9. Pipette 5ml 10. Pipette 1ml 11. Bunsen burner 12. Ice 13. Ice chest 14. Thermometer 15. pH solutions Patricia Marcel Biology 1111-17 Lab # 7 Enzymes Results: Table 2B The Effect of
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to determine the effect of varying pH on the rate of reaction catalysed/controlled by the enzyme trypsin. Method 1. Add 4cm³ of the 2% trypsin solution in to 6 test tubes labelled A-F 2. Add 4cm³ of the appropriate buffer solution to each. ( I will be testing pH 4‚5‚7‚8‚8.8 and 10) 3. Add 4cm³ of distilled water and 4cm³ of the appropriate buffer solution to 6 control test tubes labelled CA-CF to see if the pH alone will affect anything. 4. Place all test tubes in a water bath (40-45oC) and put the
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phosphate solution using a pH meter and construct a titration curve of an amino acid to determine the pka values of its ionisable groups to identitfy an unknown amino acid. Method: The ratio of [HPO42-] to [H2PO4-] required to produce buffer solutions at pH values 5.9‚ 6.9 and 7.9 were calculated. 0.1M of H2PO4- and 0.1M HPO42- were used to mix appropriate volumes to 25mL of each of the buffer solutions. The calibrated pH meter was used to measure and record the pH of each buffer solution and then
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