L-Asparagine Lab Report

The absorption of proteins as well as thrombus formation on the pH sensors has been known

The goal of this experiment was to synthesize aspirin. In this experiment aspirin, also known as acetylsalicylic acid, was synthesized from salicylic acid and acetic anhydride. In the reaction the hydroxyl group on the benzene ring in salicylic acid reacted with acetic anhydride to form an ester functional group. This method of forming acetylsalicylic acid is an esterification reaction. Since this esterification reaction is not spontaneous, sulfuric acid was used as a catalyst to initiate the reaction. After the reaction was complete some unreacted acetic anhydride and salicylic acid was still be present in the solution as well as some sulfuric acid, aspirin, and acetic acid. Crystallization, which uses the principle of

The dependent variables were the alpha naphthyl acetate esterase (ANAE) and beta naphthyl acetate esterase (BNAE) enzyme

According to the Tufts University Health and Nutrition letter the FDA supports the safety of the toxicology of Aspartame. It has been stated that "The FDA recently rejected two citizen petitions calling for an aspartame

The purpose of this experiment was to investigate the effect of protein adsorption and thrombus formation on a pH sensor in regards to its function and accuracy. [2] Different solutions of pH were first measured with a clean, calibrated sensor. Then measured again after the same sensor was exposed to a blood solution.

AAS has contributed to the understanding of elements having different absorption emission spectra due to their difference in energy levels. In the absorption spectrum, the absorbed light are shown as black gaps. As the number of electrons increase, the number of spectral lines also increase. Hence, by measuring the absorption of light, the concentration of the element within a sample can be determined. By knowing the concentrations of an element, scientists are now aware that even the smallest amount can make a significant impact towards the biological system. Therefore, scientists have brainstormed ways to monitor the use of chemicals in the

Apparatus: Spectrophotometer (UV-1201), cuvettes, water bath (set at 37°C), 200µl and 1000µl micropipettes and test tube

The absorbance is measured using a Plate reader and a Standard curve is generated. Also, the different types of pipetting techniques are assessed in this Assay.

During my experience at Asterand Bioscience in Detroit I learned about the daily activities of laboratory assistants. This experience has helped me prepare for future labs which I will do in college and hopefully in my future career. Having working in the lab and learning the new technologies of DNA/RNA isolation it has changed my outlook on pharmacists and how they use the DNA segments and gel electrophoresis to find new ways to cure diseases and find out the genes involved. I shadowed Jean Mackenzie for 17 hours during my stay at Asterand Bioscience; I enjoyed her guidance during the labs. Jean also showed me behind the scenes of the company, I was able to go to meetings and file through paper work in order to have “Tissue Tumor” be delivered.

Incorporation of assay controls included setting up a spectrophotomer and running the chart recorder with a full-scale deflection before the start of the assay. The set recorder had a corresponding value of 1 for the change in the absorbance. Therefore, prior testing was done to observe whether a change occurred in the readings. This helped to indicate that the results were valid, as they could have been affected by a fault during the setting up of the spectrophotometer. On the other hand this was considered as one of the controls for the experiment. Nevertheless, a new cuvette had to be used for each assay.

The enzymatic based sensing approached was used for the measurement of glucose and cholesterol. H2O2 was used as a recognition species that produced as a result of enzymatic oxidation of glucose and cholesterol. H2O2 quench the thiol-capped QDs fluorescence emission. The degree of quench fluorescence emission was used as a function of H2O2¬, glucose or cholesterol concentrations. The pH is an important parameter that affects the fluorescence emission of thiol-capped QDs. The thiol-capped QDs were screened for different pH range and H2O2.

Lanthanides complexes shows values of 0.1-1.0. All species exhibit excellent stability and moderate to high luminescence efficiency (quantum yields Eu = 0.050.08 and Tb = 0.300.57) in aqueous solution at physiological ph. Special focus is put onto the properties of the complexes in regard to circularly polarized luminescence (CPL) (3). The maximum luminescence dissymmetry factors (glum) in aqueous solution are high with ¬glum¬ max = 0.08 – 0.40. To calculate the standard deviation of incident light N is the # of photon counts. The standard deviation of glum is calculated by using delta=IL -IR=square root 2N. The lanthanide circulatory polarized luminescence does depend on the glum value (3,4). In CPL spectroscopy one measures the luminescence dissymmetry factor, glum, which is related to the intensity of left and right circularly polarized emitted light (3). CDL measures the difference in absorption between left (molar absorption coefficient (L) and right (R) circularly polarized light, while CPL measures the difference in emission intensity between left (IL) and right (IR) circularly polarized light (3,4). See Figure A, B, and

There is a two-step reaction for hydrolyzing phosphate monoester by PTPs. First, there is a nucleophilic attack of the cysteine (Cys) in the active site on the phosphorus atom of the target substrate. At the same time as the ester bond is cleaved, the aspartic acid (Asp) residue donates its proton to the leaving group oxygen. This reaction leaves the phosphate group covalently attached to the nucleophile via a thioester linkage. In the second step, the phospho-enzyme intermediately is hydrolyzed by a water molecule which gives the enzyme and inorganic phosphate. The conserved Asp in the first step acts as a general base to activate the water molecule and helps to hydrolyze the intermediate complex

The Biuret test is used to detect the peptide bonds that are existent in a protein. Peptide bonds can induce the Biuret reagent in a solution to turn from blue to violet. The spectrophotometer determines the absorbance of protein. Using this data, a standard curve was formulated (Stallsmith, 2014). We hypothesized that the absorbance would increase linearly with concentration.

AMC vitrigels were cast in microplate wells, vitrified, rehydrated and measured using a standard multiplate reader Synergy 2 (Biotek). Area scan measurements were made at over the visible spectrum at 50 nm intervals. Data was compiled and analyzed in Excel.