Michaelis–Menten kinetics

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  • Michaelis-Menten Kinetics

    547 Words  | 3 Pages

    that involved. In this lab, we used the Michaelis- Menten Kinetic, which proposed by two scientists Leonor Michael and Maud Leonora Menten for enzymatic dynamics. The model explains how reaction rate depends on the concentration of substrate and enzyme (chemwiki.ucdavis.edu). In the reaction of an enzyme catalyzed, the enzyme interacts with the substrate by binding to its active site to form the enzyme-substrate complex, ES. The reaction is

  • What Is The Optimum Ph And Temperature Conditions

    1391 Words  | 6 Pages

    The low Vmax could be due to an incomplete reaction. However, despite the large difference in Vmax between experimental and literature values, Figure 3 reflects similar data obtained in similar studies [9]. Michaelis-Menten graphs depicted by Figure 4 and Figure 5 show that all concentrations of oxalic acid (0M, 0.01M and 0.03M) and oxamic acid (0M, 0.0200M and 0.0600M) ) seemingly saturate at the highest lactate concentration which was 95mM. In both figures, LDH

  • Enzyme Concentration And Incubation Time

    1595 Words  | 7 Pages

    exhibits 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

  • Investigating The Amount Of Enzyme That Would Produce A Reaction Rate

    1835 Words  | 8 Pages

    After obtaining all of the absorbance values and unit conversions were calculated, as shown on page 18, a rate of product formation versus time was graphed as well as a Michaelis-Menten plot. Based upon the Michealis-Menten plot, estimated values of Vmax and Km were recorded. Instead of generating a Lineweaver-Burke plot to determine the calculated values of Vmax and Km, our lab instructor provided a video for us to watch, which allowed us to

  • Enzyme Catalyzed Reaction Lab Report

    563 Words  | 3 Pages

    Additionally, rate expressions can provide further information that can help explain the complex nature of a specific biochemical reaction3. In order to characterize an enzyme, researchers study the kinetic and molecular properties of their enzyme of interest. This can generally be done by applying the Michaelis-Menten model4. In this model, the enzyme-catalyzed reaction is described mathematically via the use of rate-equations. To measure the rate of reaction, biochemists will measure the change in absorbance

  • Aspartate And Glutamate Lab Report

    360 Words  | 2 Pages

    The central objective of this thesis is the complete In-Vitro and preliminary In-Vivo development of biosensor devices suitable to measure the excitatory neurotransmitters, Aspartate and Glutamate, within the ECF of the brain, and for the subsequent characterisation of these devices. Owing to the circumstance that both Aspartate and Glutamate are actually electro-inactive compounds, their direct electrochemical detection is not possible. As such, another means of detection was required to overcome

  • Biochemistry Ldh Assay

    3629 Words  | 15 Pages

    BIOL 3380 Name:_____________________________________ Circle Session: T-PM W-AM W-PM 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

  • Effect Of Increasing Concentration Of Yeast Invertase On Sucrose

    1083 Words  | 5 Pages

    of Submission Biochemistry Laboratory Experiment: Enzyme Kinetics Abstract The aim of the study is two-fold: to study the rate of absorbance with increasing concentration of glucose, and to measure the activity of enzyme yeast invertase on sucrose. In task 1, the product formation was measured using 3, 5-dinitrosalicyclic acid that reacts with glucose leading to a change in colour from yellow to reddish brown. In task 2, the enzyme kinetics of yeast invertase on sucrose was studied. The absorbance

  • Ap Biology Lab Answers

    593 Words  | 3 Pages

    1. Both answers are correct. There are two different models for substrate binding: lock and key or induced fit. In the lock and key model, the active site of unbound enzymes fits perfectly with the complementary shape of its substrate. In the induced fit model, the enzyme changes shape to confirm to the substrate after binding. 2. If Keq = 1, what is the ∆Go´? 0 If Keq > 1, what is the ∆Go´? Negative Exergonic If Keq < 1, what is the ∆Go´? Positive Endergonic 3. How is free energy useful

  • Enzyme Catalysis And Enzyme Inhibition Essay

    1098 Words  | 5 Pages

    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 the uninhibited enzymes are compared to those of the inhibited enzymes. Results of the experiment show that the uninhibited WT-AP and MBP-AP enzymes yielded expected kinetic constants according to a reference. However, the inhibited enzymes produced kinetics constants that did not resemble a competitive inhibition

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