An experiment to determine the amount of urea in a urine sample.Introduction.Metabolism produces a number of toxic byproducts, in particularly nitrogenous wastes resulting from the degradation of proteins and nucleic acids. Amino groups (NH2) are the result of such metabolic reactions and can be toxic if ammonia (NH3) is formed. Ammonia tends to increase the pH of body fluids and interfere with membrane transport functions. To prevent this, amino groups are converted to urea, which is less toxic and can be transported and stored for release through the excretory system. Urea is the result of two amino groups joining to a carbonyl (C=O) to form CO. (NH2)2, the process of which is called the ornithine cycle and takes place in the liver. The ornithine cycle was developed by Hans Krebs in 1932 and is similar to the Krebs cycle through the use of oxaloacetate. One of the steps in the cycle is the breakdown of arginine into ornithine and urea, a reaction catalyzed by the enzyme arginase. (See below)(Fig 1.0)Arginine Orthinine UreaUrease is the enzyme that catalyzes the hydrolysis of urea according to the following equation:(NH2)2CO(aq) + 3H2O(l)  CO2(g) + 2NH3(g)The acid ammonium carbonate forms because carbon dioxide dissolves in water to produce carbonic acid (H2CO3), which immediately reacts with ammonia to form ammonium carbonate ammonium. This is illustrated by the following equation: 2NH3(g) + H2CO3(aq)  (NH4+)2CO3(aq). The resulting solution can then be titrated against hydrochloric acid with methyl orange as an indicator to determine the amount of urea present. initially.The point of neutralization using a methyl orange indicator is determined using the following color changes. Acidic  Red. Neutral  Yellow. Alkali  Orange.Enzymes are almost all made of proteins globular. The structure of enzymes can be divided into three categories:1. The primary structure, which is the sequence of amino acids.2. The secondary structure, which is the coiling of the protein into an alpha3 helix. The tertiary structure, which is the 3D shape in which the protein is folded. This form gives the enzyme its properties and specificity. The shape is held together by ionic bonds, disulfide bridges, and weaker hydrogen bonds. Method. Six urea solutions were prepared and placed in conical flasks, including one of unknown concentration. The vials were sealed to prevent CO2 and NH3 gases from escaping, then placed in a water bath at 35°C for 1 hour..