NADH dehydrogenase

Comparing LC50 of Insectisides Pirimicarb and Rotenone on Blowfly, Blowfly larvae, Woodlice and Daphni Abstract The LC50 of insecticides rotenone and pirimicarb were compared by testing blowfly, blowfly larva, woodlice and daphnia. Rotenone is a NADH dehydrogenase inhibitor causing death by oxidative stress however pirimicarb causes toxicity through acetylcholinesterase inhibition. It was found that rotenone had large toxic effects on daphnia, blowflies and woodlice but not maggots and pirimicarb had

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

Alcohol is a very widely used drug, and is therefore present in many clinical and forensic toxicology cases. Quantitation of alcohol levels in patients affects the clinical treatment they receive as well as any legal consequences associated with the incident that led to their hospitalization. Alcohol analysis and its consequences for postmortem cases also forms a large part of the forensic toxicologist’s workload [1-2]. Although gas chromatography–mass spectrometry (GCMS) or gas chromatography

PURIFICATION OF LACTATE DEHYDROGENASE FROM CHICKEN MUSCLE TISSUE Abstract The enzyme lactate dehydrogenase (LDH) catalyzes the last step of anaerobic glycolysis that is important for the normal function of the body. Purification of LDH is essential to understand its structure and function. The purpose of this experiment was to extract and purify LDH enzyme from chicken muscle tissue using a variety of various. Analytical methods such as activity and protein assay were employed to determine

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

endurance activities. Type II is considered fast, glycolytic and even oxidative, but it is used more for sprint-related activities. In addition, phosphorylase, lactic dehydrogenase (LDH), and succinate dehydrogenase (SDH) are skeletal muscle enzymes along with myosin ATP, NADII2, tetrazolium reducatse, and alpha-gycerophosphate dehydrogenase help determine the muscle types based on these measurements. Purpose of the Study The purpose of the study is to measure the amount of these skeletal muscle enzymes

Characterization of Avian Lactate Dehydrogenase To whom correspondence should be addressed Sylvia DaoudKinze and James Proestes, Department of Biochemistry, Portland State University Professor, Portland Oregon, 97207-0751; E-mail: 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

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

is consumed, it passes from the stomach and intestines into the blood, a process referred to as absorption. Alcohol is then metabolized by enzymes, which are body chemicals that break down other chemicals. In the liver, an enzyme called alcohol dehydrogenase

quickly in individuals with a higher fat content. When alcohol is metabolized, acetaldehyde, a poisonous byproduct, is formed. Alcohol dehydrogenase breaks down alcohol into acetaldehyde. Acetaldehyde dehydrogenase further breaks down the poisonous acetaldehyde into acetic acid. Some ethnicities, such as some Asian groups, have less active acetaldehyde dehydrogenase leading to a buildup of