Glycolysis is located in the cytoplasm of the cell of plants, animals and micro-organisms. It occurs in both eukaryotic and prokaryotic cells. Glycolysis has three stages. The first stage has three different steps, phosphorylation, isomerization and a second phosphorylation reaction. Phosphorylation happens when a phosphate group is added to a molecule that is derived from ATP.
Globin- It is a protein surrounding & protecting the heme molecule. Heme synthesis: Heme synthesis is carried out in mitochondria & cytosol of the cell involving cascade of steps :- 1) The first step occurs in mitochondria, where condensation of succinyl-CoA & glycine is carried out by enzyme ALA-synthase resulting in product formation i.e. 5-aminolevulinic acid. 2) 5-aminolevulinic acid is transported to the cytosol for formation of porphobilinogen molecule. 3) After formation
Summary Endoplasmic reticulum is a eukaryotic organelle that forms interconnected network of cisternae, vesicles and tubules within the cells[1,2]. There are two types of endoplasmic reticulum: rough and smooth endoplasmic reticulum. The rough endoplasmic reticulum is covered with ribosomes in its membrane, these ribosomes are the site of protein synthesis. The ribosome free endoplasmic reticulum also know as smooth endoplasmic reticulum, its functions including lipid synthesis, drug detoxification and regulation of calcium concentration[2,3,4]. Furthermore, the endoplasmic reticulum can be isolated from animal soft by centrifugation method and the production form isolation can be used to study the metabolism of lipid and the recovery
Throughout the urea cycle, the amino acid, arginine, is changes into ornithine- this is another amino acid when hydrated, that is when water was added. During this reaction, urea is the product formed (Nelson and Cox 2008). Figure 1 shows the urea cycle, occurs specifically in the mitochondria and cytosol in the liver. (Nelson and M.Cox 2008). Urea is made in the liver by means of enzymes in the urea cycle.
It contains two binding sites that orient themselves to point towards the centre of the ring. Each subunit contains two domains; an RNA binding domain and an ATP hydrolysis domain. In Rho there is an N terminal domain and a C terminal domain where the N terminal domain contains two subdomains. These are a three helix bundle followed by a five stranded beta barrel. The six C terminal domains have a parallel beta sheet enclosed between multiple alpha helices.
2. Membrane alterations: translocation of phosphatidylserine (PS) occurs during apoptosis. Exposure of PS on the outer leaflet of the plasma membrane can be detected using Annexin V. Annexin V binds to the PS and is in turn tagged with a label such as phycoerythrin or fluorescein isothiocyanate (FITC). These labels can be detected using flow Cytometry. Alterations in membrane permeability can be detected using 7-aminoactinomycin
INTRODUCTION An important pre-requisite in order to know the function and structure of a protein is called protein purification (Berg et al., 2002). It is the process of removing protein contaminants and also to be able to transfer proteins to a stable environment in a form that is required for its’ use (Queiroz et al., 2001). There are different techniques available today for protein purification such as precipitation, which uses a neutral salt for purifying, filtration and chromatography to name a few. One may choose which technique to use depending on the intended use of protein however, it is chromatography that is widely used today because of its’ high resolving power (Saraswat et al., 2013). It can purify any soluble substance with the aid of a right adsorbent material and carrier fluids.
coli reacts with the CoA affinity. The synthesis of succinyl CoA is thought to occur at an active binding site in the case of E. coli. If ATP binds at the second active site, there is formation and release of the Succinyl CoA at the initial site. Binding of ATP at the second site causes the site to undergo phosphorylation. ATP, magnesium ions, the enzyme, and phosphate incubated in the presence of hydroxylamine trapping succinyl CoA and pyruvate kinase-lactate dehydrogenase ADP.
The lock and key hypothesis states that, the substrate fits exactly into the active site of an enzyme which is responsible for biological events to take place. The induced fit hypothesis states that the shape of the enzyme changes as the substrate molecule approaches it. Then, the substrate fits into the enzyme, thus forming a complex. The enzyme regains its original shape after particular biological events are catalyzed by this enzyme-substrate complex. Mechanisms of enzymes used to lower Activation energy: The enzyme has some amino acids in the active site.
These protease enzymes will catalyze the breakdown of the protein into amino acids throughout the stomach and small intestines. Once broken down into amino acids, the microvilli will absorb them and will send them into our cells. Inside the nucleus of the cell, a DNA molecule will be unjointed by a RNA polymerase enzyme (brought by proteins), starting a process called transcription. This process allows RNA molecules to copy the genetic information from the unjointed DNA. The RNA polymerase begins by binding itself to the first base of a gene then it starts to copy the genetic information to a RNA molecule called a Messenger RNA (MRNA).