Arginase Lab Report

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INTRODUCTION:
Arginase is an enzyme- enzymes are biological catalyst which drives a reaction at the speed of life. Arginase is a hydrolase, hydrolases catalyze hydrolysis reactions, this is determined via the E.C number (Nelson and Cox 2008). Arginase has the EC number is 3.5.3.1 (Schomburg 2015). The enzyme ‘commission number’ is the arithmetical classification that is used for enzymes which indicates the chemical reaction they catalyze. EC 3 are hydrolases, which forms two products from the substrate via hydrolysis. (Bach, et al. 1961) This is seen in the equation: L- Arginine + H2OL-Ornithine + Urea (Nelson and Cox 2008).
The urea cycle is the procedure where ammonia is transformed into to urea. 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. The enzymes that is associated with the urea cycle are; carbamoyl phosphate synthesase,
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The reaction that occurs can be investigated via the adding of the liver extract which contains the arginase to urea concentrations and distilled water. The amount of urea formed is determined via spectrophotometric analysis α-INPP. The urea produced was known via the color reaction with the α-INPP, it is the reagent used for the colorimetric determination of urea. (Barry J, et al. 1984). The red color formed when the α-INPP is reacted with the urea, is sensitive to light thus it is photo labile. The absorbance level @ 520 nm obtained from the spectrometer indicates the amount of urea obtained via measuring the absorbance of the light through the supernatant coloration, which was provided by the

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