NADH dehydrogenase

INTRODUCTION: Lactate dehydrogenase (LDH) is a tetrameric molecule categorised into several types, which are known as isozymes or isoenzymes. LDH activity is commonplace in all tissue and can be seen in higher quantities in the blood when tissue damage is present due to enzyme leakage, typically seen in myocardial infraction or liver disease (1, 2). LDH consists of either a heart (H) or a muscle (M) type subunit and can be made up collectively where five different proteins may be produced H4, M4

absorbance change when the substrate is converted to product by the enzyme. If we use the product of the citrate dehydrogenase reaction in a second reaction that does have an absorbance change we can measure the success of the initial reaction. This is known as coupling. Malate dehydrogenase is assayed by measuring the change in absorbance of NADH when it is reduced to NAD+ when malate dehydrogenase coverts oxaloacetate to L-

Chloroplast can capture sunlight with the help of chlorophyll pigment and is responsible for photosynthesis. Photosynthesis is divided into light and dark reactions: a) Light reaction (Photosynthetic electron-transfer): The electrons in chlorophyll is energized by sunlight causing electron movement along electron transport chain in the thylakoid membrane. Chlorophyll obtains electron from water, H+ is pumped across thylakoid membrane resulting in the synthesis of ATP. Similarly, there high energy

ATP ========== ADP +P+ H+. This reaction takes place in the presence of ATPase enzyme. This H+ can be buffered by Creatine: CrP + ADP + H+ ====== ATP + Cr. This reaction takes place in the presence of Creatine kinase enzyme. Lactate: Pyruvate + NADH+H+==== Lactate + NAD. This reaction

ABSTRACT: Lactate dehydrogenase (LDH) is considered to be a major checkpoint for an anaerobic glycolysis by catalyzing the pyruvate to the lactate. By isolating lactate dehydrogenase from a homogenized chicken breast from a local marker, further examination of kinetics was able to be seen. Three tests were ran over a course of four weeks, which involved ldDEAE fractions as well as Affinity fractions. Gel electrophoresis was used to check the purity of the LDH and it was found that the purification

The Krebs cycle also known as the Citric Acid cycle, is the second part of the three steps in which cellular respiration happens. The Krebs cycle was discovered and named after Hans Krebs, a German scientist. The Krebs cycle takes place in the mitochondrial matrix of the cell, occurring between glycolysis, which breaks down glucose turning into pyruvate, and oxidative phosphorylation, which is what creates ATP. This is processes where the body harvests energy from the food we consume. The Krebs cycle

The energy is released in this process. This energy is converted into atp and nadh. Ths process is enzyme controlled process but Some times glycolysis cocome uncontrolled so it is regulated by enzyme inhibitors. That are discussed here. Inhibitors of glycolysis: In this process of respiration isocitrate dehydrogenase enzyme act as the most important inhibitor this inhibitor inhibits the enzyme that produces the product. This process occurs because

Cellular respiration is a chemical oxidation-reduction reaction that provides the energy needed for a cell to function. A chemical species that gives one or more electrons is a reducer. When a reducer loses electrons, it oxidizes. When an oxidizer picks up electrons, it is reduced. These reactions are called oxidation-reduction reactions. Cellular respiration is therefore carried out in three stages, this is glycolysis (this is also the first stage of fermentation), the Krebs cycle (second stage)

Enzymes Enzymes are catalysts. Most are proteins. (A few ribonucleoprotein enzymes have been discovered and, for some of these, the catalytic activity is in the RNA part rather than the protein part. Link to discussion of these ribozymes.) Enzymes bind temporarily to one or more of the reactants of the reaction they catalyze. In doing so, they lower the amount of

On the graph describing how the different preincuabated temperatures affect the LDH1 enzymes we can see that test tube 2 and 3 have high absorbance’s which indicate that there is a high metabolic activity at the temperatures of 37°C and 44°C. However when we preincubate the enzymes at 50°C the enzyme activity starts to decrease and the absorbance is test tube 4 is 0.850. From test tubes 4 to 6 the decline is not very sharp as seen from the graph which suggests that the LDH1 enzyme still works between