Full Report on Exercise 4.2 ESTIMATION OF PROTEIN CONCENTRATION BY SPECTROPHOTOMETRY And Exercise 4.3 GEL FILTRATION CHROMATOGRAPHY Joel Don M. Untalan CHEM 160.1 – 1L AY 2013 – 2014 Groupmates: Sonette Yao Kristopher Quilan Laboratory Instructor Carmelo C. Briones I. Introduction Analyzing proteins in determination of protein concentration by spectrophotometry is important. It determines to what concentration of a certain protein is in a crude sample. In this technique‚ a wide
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Gel filtration GEL FILTRATION OF PROTIENS Aim: The aim of this experiment is to identify proteins from a complex mixture using the gel filtration technique also known as size exclusion chromatography. This technique is widely used by biochemists when proteins larger than the pores are excluded from the column and the smaller molecules elute last and then collected in test tubes for examination by spectroscopic techniques. The red/brown proteins‚ in particular‚ will be observed closely
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Abstract The activity of invertase and the quantification of albumin and casein were performed and analyzed after extraction of the said proteins from their respective sources. Isolation of proteins was initiated by the breakage of the cell wall / membranes in three different ways. Homogenization of invertase‚ albumin and casein were achieved via grinding process‚ addition of 1M acetic acid and acidification by 0.1M hydrochloric acid correspondingly. Extraction of invertase and casein involved
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Experiment B2 Chromatography for Protein Purification Name Matric No. Group : : : Date of Expt. : GRADE : A. Learning objectives 1. 2. 3. 4. Establish chromatographic assay to determine protein concentrations in a mixture. Appreciate the importance of resolution in protein chromatography. Understand the tension between purity and yield in protein chromatography. Understand the importance of mass balance closure in protein purification. B. Introduction I. Fast Protein Liquid Chromatography
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EXPERIMENT NO. 15 PROTEIN CHARACTERIZATION BY ELECTROPHORESIS Abstract The molecular weights of protein extracts were assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Two sets of four protein samples‚ standard bovine serum albumin (BSA)‚ invertase‚ egg albumin‚ and casein‚ were prepared; one set containing β-mercaptoethanol (BME) while the other did not. These were then analyzed through SDS-PAGE with 12.5% resolving gel‚ prepared using 2 M Tris-HCl at pH 8
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Introduction Methionine and cysteine are both sulphur containing amino acids. Most proteins will contain one‚ or both of them at some point in the polypeptide chain. As such‚ many amino acids contain sulphur in some form‚ which is required in small amounts in the mammalian diet. Methionine has a thioether side chain‚ and cysteine’s contains a thiol group. These side chains exist as free thiols inside the cell‚ and are oxidised causing them to pair up and form disulphide bonds in an extracellular
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EXTRACTION AND CHARACTERIZATION OF PROTEINS Abstract Different techniques and principles for protein extraction and characterization were demonstrated in this experiment. Various proteins were extracted from different sources: 1.67 g yeast invertase‚ 1.03 g egg white albumin‚ and 5.15 g of milk casein. Activity assay for invertase was performed using Benedict’s test and the enzymes inverting action on sucrose was confirmed. Warburg-Christian Method and Bradford Assay were also employed to determine
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Question 1 1.1 Silica gel chromatography: This is known as the stationary phase in column chromatography. Firstly‚ the tapered exit of the column is sealed using porous material. This porous material serves as support for the packing material‚ and prevents it from exiting the pipe. Thereafter‚ silica gel is compacted into the glass pipe to make the separating column. In finishing preparation of the column‚ the solvent which is used as the mobile phase is then passed through the dry column. Then the
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Abstract The experiment‚ entitled Extraction and Characterization of Proteins‚ aims to isolate casein from milk and albumin from egg; to explain the methods employed for protein extraction; to apply spectrophotometric methods in characterizing and quantifying extracted casein and albumin. The experiment was divided into 2 parts; the extraction of Albumin from egg and the determination of protein concentration via the Warburg-Christian method and Bradford Assay method. In the first part‚ egg
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Protein Hydrolysis and Characterization Group 7 Niez‚ Robert Francis‚ *Orbin‚ Alfonso Ricardo* Parro‚ Athena Emmanuelle Peralta‚ Christian Department of Biological Sciences‚ University of Santo Tomas‚ Manila‚ Philippines • Abstract Hydrolyzed Protein is protein that has been hydrolyzed or broken down into its component amino acids. While there are many means of achieving this‚ two of the most common are prolonged boiling in a strong acid (acid-HVP) or strong base or using an enzyme such
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