Succinate dehydrogenase

Introduction: A variety of alcoholism cases develop from factors that cause an individual to develop alcoholism. These two factors are genetic factors as well as environmental and risk factors. About 50 percent cases of alcoholism are related to genetic factors and the remaining 40 percent is related to risk and environmental factors. In the article Mary - Anne Enoch acknowledges that “there are gene to gene as well as gene and environmental interactions underlying a disorder such as alcoholism

Cardio- Nephroprotective Effects of Guava and Olive Leaf Extracts on Doxorubicin-Induced Toxicity in Rats Abstract Objective: Doxorubicin (DOX) is an anticancer drug that is known to increase oxidative stress in several organs. Our objective was to evaluate the possible cardioprotective and nephroprotective effects of guava leaf extract (GLE) and olive leaf extract (OLE) on DOX-induced toxicity in rats. Methods: Forty adult male albino rats were randomly divided into 4 groups of 10 rats each, as

Lactate dehydrogenase (LDH) is an enzyme that catalyzes the reaction of glycolysis. It is responsible for the metabolism of carbohydrates, principally glucose, catalyzing interconversion of lactate and pyruvate with nicotinamide adenine dinucleotide as coenzyme (Heinová, Kostecká & Csank, 2015). Under aerobic conditions, pyruvate arrives the mitochondrial matrix and will be transformed into acetyl-CoA (Wei, Wei, Li, Xu & Wei, 2015). LDH can be found in both plants and human. LDH has two unique subunits

Utilizing Acetone Powder of Several Organs to Compare Specific Proteins and Measure L-Lactate Dehydrogenase Activity Abstract Animal organs contain a diverse amount of proteins that define their function. In this study, acetone powder solutions of calf liver, bovine pancreas, chicken muscle, porcine kidney, porcine brain, and porcine heart were analyzed through an SDS-Page gel to determine diversity of proteins and through an LDH assay to determine enzymatic activity. It was found that chicken

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

The Mathematics of Blood Alcohol Concentration As I approached my sixteenth birthday, I began to study for my G1 written test in order to receive my drivers’ licence. While doing a practice test, I came across a statistic that stated, “In the United States in 2013, it was estimated that 10 076 people were killed in crashes that involved one or more drunk drivers and 290 000 people were injured in these accidents ”. I had heard a variation of this statistic many times, however I didn’t truly grasp

L-Lactate Dehydrogenase L-lactate dehydrogenase, or LDH, is an oxidoreductase that occurs in many organism and is a reaction that is important to many cells. From the peptide sequence, this specific enzyme catalyzes the pyruvate to lactate reaction along with the coenzyme NAD+/ NADH. The enzyme classification for this sequence is EC: 1.1.1.27, these numbers each identify a specific part of the enzyme and the reaction is a part of. The first one identifies that this is and oxidoreductase reaction

Figure 5 - Michaelis Menten Graph of Ethanol (pH 9.0) Representing the Velocity versus Substrate Concentration. Different concentrations of ethanol were used, and the absorbance reading taken through enzyme kinetics. The velocity was calculated through the conversion of the slope of the data points to abs/min. K_m was found to be 5.76×〖10〗^(-3) M, V_max 1.71×〖10〗^(-3) M/min, K_cat 2.85×〖10〗^(-2) 〖min〗^(-1), and K_cat/K_m 4.94 〖min〗^(-1) M^(-1). Figure 5 - Michaelis Menten Graph of Ethanol (pH

care of whatever alcohol is left in the body. Alcohol in beverages is known as ethyl alcohol, more commonly known as ethanol. This ethanol is chemically broken down in the liver. The enzyme, alcohol dehydrogenase, strips electrons from the ethanol to form acetaldehyde. Another enzyme, aldehyde dehydrogenase, with the help of oxygen, will convert the acetaldehyde into acetic acid. The acetic acid can be used for to form fatty acids or if further broken down into carbon dioxide and water. The rate at

An alternative approach of affinity chromatography with extremely significant results is dye-ligand affinity chromatography. In this type of affinity chromatography, dyes compose the group of ligands than are employed in the technique (Hage et al., 2012). The initial motivation for scientists to investigate more about dye ligand affinity chromatography was given after the interactions that took place between Blue Dextran, a Cibaron Blue and dextran conjugate, which is used as a void marker in size-exclusion