......3 Introduction.............................................................................................5 Mechanisms of Fibrinolysis.......................................................................6 Different methodologies/Assays to Detect Fibrinolysis...................‚‚.......12 Venous Thromboembolism; Pathophysiology‚ Clinical features and Diagnosis.....................................................15 Materials
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Table of Contents 1 Table of Contents 2 2 Introduction 4 3 Experimental Procedures 5 3.1 Sample preparation 5 3.2 Initial Extraction of Acid Phosphatase 5 3.3 Determination of Protein Concentration by the Folin-Lowry Assay 5 3.4 Specific Activity Assay 6 3.4.1 Definition of Enzyme Unit and Specific Activity- 6 3.5 Determination of pH Optimum 6 3.6 Determination of Michaelis-Menten Constant 7 3.7 Ammonium Sulphate Fractionation 7 3.8 Gel Filtration on Sephadex 7
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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‚ which showed the enzyme activity concentration of the 60% sup was less than 1/3 of the 40% cut. The purification factor
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VIDAS Vitek Immuno Diagnostic Assay System VIDAS principle • Based on specific antibody and antigen reaction • Antigen = pathogen or its components in the sample See notes VIDAS substrate • One of the antibodies used has an enzyme covalently linked to it ⇒antibody-enzyme conjugate Colored product or light antibodyenzyme conjugate • Antigen detected by enzyme assay – Substrate added is converted to a colored or fluorescent product antigen Components of VIDAS System •
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Mam Dawn Assay of HCL Aqueous Alkalimetry Direct titration 0.1N NaOH Methyl Red TS HCL + NaOH NaCl + H2O Assay of Diluted H3PO4 Aqueous Alkalimetry Direct titration 0.1N NaOH Thymolphthalein TS H3PO4 + 2NaOH Na2HPO4 + 2H2O Assay of H3BO3 Aqueous Alkalimetry Direct titration 0.1N NaOH Phenolphthalein TS H3BO3 H+ + BO2- + H2O Assay of Tartaric Acid Aqueous Alkalimetry Direct titration
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During this experiment‚ the method of Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE) was conducted using a negatively charged protein and pre-stained molecular weight markers. The hypothesis was that the molecular weight of N-acetyl-β-D-hexosaminidase B would be 28‚000 kDa. To confirm or reject the hypothesis‚ the molecular weight of N-acetyl-β-D-hexosaminidase B and the concentration of protein had to be determined. The electrophoresis of the protein gel were conducted using
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The Lowry protein assay is a biochemical assay for determining the total level of protein in a solution. The total protein concentration is exhibited by a color change of the sample solution in proportion to protein concentration‚ which can then be measured using colorimetric techniques. It is named for the biochemist Oliver H. Lowry who developed the reagent in the 1940s. His 1951 paper describing the technique is the most-highly cited paper ever in the scientific literature‚ cited over 200‚000
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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 The treated and untreated samples were measured using Bradford assay. 10µl of the samples were made up to 100µl with distilled water. 30µl of the diluted samples was mixed with 1.5ml of Bradford reagent and incubated for 10 minutes before measured
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ID: 5220710 Lab Section: 34 Date Experiment Performed: Sept. 26th‚ 2012 Lab Partners: K. Cloutier J. Yang ABSTRACT Protein concentration analysis is primarily done through an accepted form commonly referred to as the Bradford Protein Assay. The main purpose of this experiment was to observe and record the various protein samples’ absorbency values through the calibrated readings of a spectrophotometer (595 nm calibration). Using the standard curve equation (y = 1.6147x + 0.0968) derived
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Question 5: The chromophore in this assay is Coomassie Brilliant Blue dye. Question 6: It is important to set up a blank to separate the solute (saline) from the protein (stock). By subtracting the absorbance of the blank (which has no protein present) from the original absorbance the absorbance of the protein at each concentration will remain. Question 7: The Lowry method relies on two different reactions. The first is the formation of a copper ion complex with amide bonds‚ forming reduced
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