Enzyme assay

three trials conducted on Horseradish Peroxidase Enzyme Assay (A405). With each trial it was determined that the amount of enzyme, in the overall 3000 ul assay solution, heavily affected the rate of the initial velocity (umol/min) for the different concentration of enzymes to catalyze each reaction hence the increase or decrease of the speed of an individual reaction by comparison. It was determined that a higher concentration of enzymes in the assay caused the rate of catalysis to sharply increase

Enzymes are biological catalysts that are involved in important pathways that allow the chemical reaction to occur at higher rates than would be possible without the enzymes. Enzymes are globular proteins that are responsible for biochemical reactions within cells and microorganism, these large proteins have more than one substrate binding sites allowing larger volumes of products to be produced. Enzyme assays are fundamental tools for measuring cellular activity and for monitoring enzyme protein

The major use of Enzyme Linked Immunosorbent Assay (ELISA) is to titrate antibodies against specific antigens (Crowther, 1995). This method involves an enzyme, which reacts with a colourless substrate to form a coloured product, is covalently linked to a specific antibody that recognises a specific antigen. If the antigen is present, the antibody-enzyme complex will bind to it, and the enzyme component of the antibody-enzyme complex will catalyse the reaction which results in a coloured product (Berg

detected [1]. With these consequences in mind, it is imperative that the test used to measure ethanol levels is reliable and accurate. If there is a possibility that the enzymatic assays used widely throughout hospitals can be inaccurate under certain conditions, it is necessary that the users and interpreters of those assays know that interference can occur and when it might happen. If markers can be developed to determine when further testing for ethanol should be done, the reliability of the test

Purification of Lactate Dehydrogenase Results and Discussion Monitoring Assays Enzyme activity assay and Bradford dye binding protein assay was used. Ammonium Sulfate Fractionation In order to isolate and purify Lactate Dehydrogenase (LDH), we first extracted LDH from bovine muscle tissue. We minced 8 grams of meat and homogenized using blender. The homogenate was centrifuged and the pellet consisting of membranes, organelles, cytoskeletal components and structural fragments was

were also running daily before testing the samples to re-set the configuration. The machine was serviced and maintained routinely and worked in good condition. 96-well U-bottom white polypropylene plate (Grenier®) was used for fluorophore loading assay and particle washing. The 1.5ml polypropylene reaction tubes (Grenier®) were used for general particle treatment and protein coupling. Also, tube magnet and plate magnet were used in particle separation. All the consumables were routinely used in Anteo

Laboratory diagnosis The clinical signs of BVDV infection are highly variable and there are many factors that affect severity of infection like viral strain, age of affected animals, immune status, reproductive stage and mixed infection. Therefore, diagnosis based on history, clinical signs and postmortem examination should be considered only as preliminary diagnosis. The accurate and confirmatory diagnosis of BVDV infection depends only on laboratory diagnosis. 1- Virus isolation BVDV isolation

Enzyme-linked immunosorbent assay (ELISA) Lab Report Abstract The enzyme-linked immunosorbent assay (ELISA) is a common laboratory technique used to measure the concentration of an analyte (usually antibodies or antigens) in solution. In the practical anti-BSA antibodies that had undergone serial dilutions were added to a BSA solution in an ELISA plate with goal of seeing how the concentration of anti-BSA antibodies would affect the colour change of the BSA solution. The results clearly

treating type 2 diabetes mellitus (T2DM) due to their suspected tyrosine phosphatase 1B (PTP1B) inhibitory activity. A new series of bromophenol analogues will be synthesised and their PTP1B inhibitory activity will be tested in in vitro enzymatic assays to elucidate their mechanism of action as PTP1B inhibitors. Background and Introduction Type 2 diabetes mellitus (T2DM) is a metabolic disease that is caused by insulin resistance of the peripheral tissues and impaired insulin secretion of the pancreatic

Introduction In this experiment, the enzyme Luciferase (Luc) was purified using differential centrifugation, precipitation, and a simplified chromatography procedure, followed by an enzyme activity assay using the enzyme’s natural substrate, Luciferin, to confirm the presence of Luc. Luciferase is a 61 kD enzyme naturally found in the tails of fireflies, a member of the Lampyridae family. Luc acts as a catalyst in an oxidation-reduction reaction with Luciferin, which allows these insects to exhibit