Synthesis Of Kestoses Lab Report

To 0.05 ml of carbonate buffer (0.05 M, pH 10.2) and 0.5 ml of EDTA (0.49 M) was added. The reaction was initiated by the addition of 0.4ml of epinephrine and the change in optical density/min was measured at 480nm. SOD activity was expressed as units/mg protein change in optical density/min. 50% inhibition of epinephrine to adrenochrome transition by enzyme is taken the enzyme unit. Calibration curve was prepared by using 10 -125 units of

H and S were diluted 20x and P1 and P2 were diluted 2x to make up a total volume of 1ml each. 50ul of each diluted sample was pipetted into 8 wells of the microplate and 50ul of each protein standard was pipetted into 2 wells. 50ul were incubated with 50ul of alkaline copper reagent. 50ul of alkaline copper reagent was added to every well containing water, buffer, sample or standard and was incubated for 30 minutes. 100ul of Folin reagent was added to the wells and incubated for another 20 minutes.

NOTE: Record the grams of gasoline, kerosene, and lubricating oils that are present in the 50 mL of crude oil. ➢ Select the flask, and choose Heating Mantel option afterward select Max Heat and make sure you record the temperature when you see crude oil begins to boil. ➢ When the crude oil begins to boil, Make sure you turn the temperature down to 60% by decreasing the heating metal two times. Step 3: Record the

P. agarwal and co-workers work for protein chemical modification by conducting a pictet-spengler reaction between aldehydes and alkoxyamines. This forms an oxyiminium ion as an intermediate that eventually undergoes intramolecular C-C bond with indole nucleophile to form an oxacarboline product. As compared to the oxime and hydrazone conjugates, the oxacarbolines are very much stable towards the hydrolysis under physiological relevant conditions as depicted by their experiment. In order to use this strategy for site specific chemical modification of formylglycine and glyoxalglycine-functionalized, they use an aldehyde-tagged variant of the Herceptin( a therapeutic monoclonal antibody). All the experiments performed by them showed that the Pictet-spengler reaction has a bright future in the research for the

Malate dehydrogenase: Malate dehydrogenase (MDH) is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate by using NAD+ and vice versa and this is a reversible reaction. Malate dehydrogenase is not to be confused with malic enzyme, both are different enzymes malic enzyme which catalyzes the conversion of malate to pyruvate and producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, in which the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is based upon pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. The malate dehydrogenase reduces it to malate, and it then traverses the inner mitochondrial membrane to get the oxaloacetate out

Each of the analyte will have its own Rf value under certain circumstances. The separation of the phospholipid classes can be improved by two-dimensional chromatography. This technique requires developing the TLC plate in a direction, then dried, and developed in a solvent mixture at a 90 ° the first development (Singh and Jiang,

This solution was diluted with diluents to gae a concentration of 0.1 mg/ml solution each of Amoxicillin trihydrate. The HPLC method was applied to the solutions and the results obtained were shown in table 4.6.11. System suitability solution: 25.0 µg/mL each of of USP Amoxicillin RS in Diluent. Precision

The absorbance of the mixture was measured at 30s (A1), 5min and 6min intervals. The value A2 was obtained by averaging the values of the 5th and 6th minute. iii. Calculation (A1-A2)sample/control Urea concentration = 15.4 mmol/L X (A1-A2)standard Creatinine concentration = 313 mmol/L X (A2-A1)sample/control

acetyl CoA + ATP + HCO-3 □(⇔┴( BIOTIN ) )Malonyl CoA +ADP+ Pi This is designated as Bi, Bi , Uni, Uni, ping pong mechanism because first two substrates add to the enzyme, then two products are released, then another substrate adds and the final product is released. Acetly coa carboxylase catalyzes coupled reaction. That is it mediates the energetically unfavourable formation of a carbon-carbon bond by coupling the reaction to the structurally unrelated but energetically favorable hydrolysis reaction of ATP to ADP and inorganic phosphate. To determine the order of the additions of substrates and products in a multisubstrate, multiproduct enzyme system generally requires a variety of experiments, including detailed kinetic analysis of the reaction rates with all but one of the substrates and products set at fixed concentration while one substrate or product is varied. The equilibrium constant for the binding of substrates and cofactors alone and in the presence of others, product inhibition kinetics and other measurement all can contribute to determining the type of the

When the results for the first test tube were recorded, then the next solution/mixture was prepared. The second test tube was exactly the same as the first, the only difference being that the SPM was this time set to 35oC. The temperature of the SPM gets increased by 1oC for every test tube solution, until test tube 7 with an SPM temperature of 40oC. After all the absorbencies for the varying temperatures had been recorded – the product concentration of each test tube solution was calculated using the absorbency readings at 10 minutes for each respective test tube mixture. The product concentration was calculated using Beer-Lamberts’ law of A = ECL.