Enzyme kinetics

Chemical Kinetics is the branch of chemistry that studies the speed at which a chemical reaction occur and the factor that influence this speed. What is meant by the speed of a reaction is the rate at which the concentrations of reactants and products change within a time period. Some reactions occur almost instantaneously, while others take days or years. Chemical kinetics understanding I used in the process of designing drugs, controlling pollution and the processing of food. Most of the time chemical

and measure the enzyme activity of β-galactosidase in the different concentrations of o-Nitrophenylgalactoside (ONPG) using a spectrophotometer. The spectrophotometer was also set at 420nm, a wavelength which is best for recording the absorbance values for the experiment. From the results, 0.9mM ONPG solution has the highest absorbance and 0.1mM ONPG solution has the least. Also, 0.5mM ONPG solution has the highest rate of enzyme activity and it is the most efficient as the enzyme activity of the

significance of result 17 Conclusions 18 References 18 Introduction Aim: to determine the kinetic parameters of the enzyme Alkaline phosphatase General Background Alkaline Phosphatase is a group of enzymes found in certain tissues (including the bile duct, bones and the liver). Based on its specific location each enzyme will present with a different structure. The highest concentration of the enzyme is found in the liver, and so is used as a liver function test

Abstract: This experimentation was to evaluate absorbance and the reaction rate of an enzyme, '-amylase in starch-iodine solution. We will be testing the relationship between enzymatic reaction affected by temperature and pH. Through the testing the enzyme at different temperatures, and different pH levels; it would determine at which temperature and pH level the enzyme worked the most efficiently. Analyzing absorbance of the solutions with spectrophotometery will determine the reaction rate. To

and measure the enzyme activity of β-galactosidase in the different concentrations of o-Nitrophenylgalactoside (ONPG) using a spectrophotometer. The spectrophotometer was also set at 420nm, a wavelength which is best for recording the absorbance values for the experiment. From the results, 0.9mM ONPG solution has the highest absorbance and 0.1mM ONPG solution has the least. Also, 0.5mM ONPG solution has the highest rate of enzyme activity and it is the most efficient as the enzyme activity of the

R-AM R-PM F-AM F-PM Experiment 9 – Pre-lab Homework Enzyme Kinetics of LDH This pre-lab homework assignment is due at the beginning of your lab session. You are provided with the following portion of a protocol: • Determine concentration of enzyme stock solution, if unknown, by taking an A280 nm reading of a 1:100 dilution (in water). Use a total volume of 1 ml in the cuvette. • Dilute some of the enzyme stock with buffer A to make a 4 mg/ml solution. • Serially dilute

Michaelis-Menten kinetics. This was determined by first deciding the optimal enzyme concentration and incubation time, 1.32*10-5 μM/mL and 60 mins, respectively. The enzyme was then reacted with varying concentrations of 4-nitrophenyl-N-acetyl-B-D-glucosamine enzyme substrate and a Michaelis-Menten plot was generated. Once it was determined that N-acetyl-B-D-hexosaminidase follows Michaelis-Menten kinetics by exhibiting a hyperbolic curve, a Lineweaver-Burk plot was generated and kinetic parameters Vmax

The aim of this paper is the kinetic analysis of mushroom tyrosinase to study the stereospecificty in its action on both L and D DOPA as substrates. It is also the aim of this paper, to carry out a kinetic study of various inhibitors on tyrosinase activity to determine their mechanism of inhibitory effect. EXPERIMENTAL Methods & Materials The procedure followed for this experiment can be found in: J. Moldovan & B. Nilson, (2010), Lab 4 – Enzyme Kinetics, UBCO BIOL/BIOC 393, UBC Vista accessed

sylviakinzie@gmail.com and proestoj@gmail.com ------------------------------------------------- Keywords: Lactate, Dehydrogenase, Avian, Bradford Assay, Affinity Column Background: Lactate Dehydrogenase also known as LDH is an important NADH dependent enzyme in metabolism that catalyzes the conversion of Pyruvate to Lactate. Results: Catalytic activity was detected from chicken breast muscle Conclusion: Copious amount of catalytic activity was detected, indicating that

Enzyme catalysis and enzyme inhibition are two essential biological mechanisms of organisms. In this experiment, WT-AP and MBP-AP enzyme are reacted with different concentrations of PNPP substrate in SpectrovVis time based assays. From the change in absorbance over time data, and the rates of the reactions are calculated, followed by the determination of the kinetic constants. Then, the MBP-AP assays are repeated with two different concentrations of phosphate inhibitor and the kinetic constants of