Succinate dehydrogenase

Succinate Dehydrogenase Activity of Mitochondria Student Name: Lolwa Alfouzan SMU Id Number: A00423662 Date:16, November 2017 Lab time: 2:30-5:29 Biol2321(cell biology) Lab Section:(01) Lab (7) Full lab report INTRODUCTION: Mitochondrion produces the energy that cell needs by breaking down sugars, fatty acids and amino acids to CO2 and H2O. In this process, which is called cellular respiration, the chemical energy in sugar, fatty acid and amino acid molecules is captured as ATP. Krebs

percentage distribution of each enzyme in each fraction (Watson, 2016). The first enzyme marker used was Succinate Dehydrogenase which catalyses the oxidation of succinate to fumarate in the tricarboxylic acid cycle (Hollywood, et al., 2010). This cycle occurs within mitochondria and succinate dehydrogenase is specifically found within the inner mitochondrial membrane. Therefore, succinate dehydrogenase activity is an indicator of mitochondrial activity (Berg, et al., 2007). Mitochondria are large organelles

Introduction In this Succinate Dehydrogenase (SDH) project, we were expected to learn the process of cell fractionation, the importance of the Bradford assay, how enzymes work what factors affect them, how to adequately micropipette, how to generate a proper hypothesis and test it, and finally, interpret our results and write a conclusion which answers the central question of this lab: how will the assigned reagent affect SDH activity? The SDH project was completed over a span of three weeks, where

measure succinate dehydrogenase activity in the tricarboxylic acid cycle of cauliflower mitochondria by monitoring the reduction of an artificial electron acceptor. Succinate dehydrogenase catalyzes the oxidation of succinate to fumarate. FAD, a coenzyme to succinate dehydrogenase, carries the hydrogens from succinate and delivers them to the electron transport chain. This enzyme complex is referred to as E-FAD. Two hypotheses were tested: 1) the higher the enzyme (succinate dehydrogenase) concentration

Succinate dehydrogenase and its coenzyme flavin adenine dinucleotide (FAD) are the only enzymes that are not located in the matrix of the mitochondrion in the tricarboxylic acid cycle. Succinate dehydrogenase is found in the inner membrane of the mitochondrion where it catalyzes the conversion of succinate to fumarate. The electrons and protons that are taken off from the succinate are transportedto ubiquinone (coenzyme Q), a part of the electron transport chain. Malonate is a strong competitive

the precision of the techniques used for isolation, by the assaying of a specific enzyme known as succinate dehydrogenase. Succinate dehydrogenase, an enzyme, is chosen due to the fact that it is almost exclusively found in the mitochondria. Thus by testing for it in the various cell fractions, we can observe just how precise the isolation techniques were. Unless contaminated, the succinate dehydrogenase enzyme should only be found in the mitochondrial faction; which indicates flaws in the isolation

Succinate Dehydrogenase Assay of Fractionated Liver Cells UC Merced Kuse, Quintin Bio 2, section #1 7/13/15 Lab Partner:De La Cruz, Natalie Abstract / Introduction / Methods / Results / Discussion / Conclusion / References / Questions Total /100 Abstract Within eukaryotic cells, there are specialized subunits called organelles, which have their own special function for the cell. These organelles usually have their own lipid bilayer, which closes them off from the rest of the cell. In order

separated and analysed by Subcellular fractionation using homogenisation and then centrifugation to separate the cells into the subcellular fractions. When the fractions are separated succinate dehydrogenase is used to identify mitochondria. Succinate dehydrogenase is an enzyme that catalyses the oxidation of succinate to fumarate in the Krebs cycle and is usually on the mitochondria inner membrane and not found in other organelles in the cell(Rustin, Munnich, and Rötig, 2002). Care needs to be taken

functions, without the presence of TEO, FAD functions normally by grabs the hydrogen from Succinate and form FADH2. However, when TEO is present such inhibitor serves as a negative feedback (Shen, J.T.et. al. 2006). When too much Ubiquinone were produced, and not enough electrons are transferred fast enough to form ubiquinol, the excessive Ubiquinone can oxidize TEO to oxaloacetate (OAA) . OAA then inhibits succinate oxidation. TEO binds to FAD functions to inhibit in the form of Oxaloacetate the flavin

Succinate Dehydrogenase and the Inhibitory Effect on its Specific Activity by Malonate By: Danielle Santiago, Nikita Shah, Zachary Voigt, Roseline Oyebanji Introduction This experiment is used to determine the level of succinate dehydrogenase (SDH) activity in a variety of reactions. Mitochondrion from a sample of cow liver is isolated via differential sedimentation and a Bradford Assay is performed to determine the concentration of SDH in the sample (Week 1 Recitation, 2013-2014). The ultimate