DENATURATION OF PROTEINS Abstract The experiment was done to be able to understand how various denaturants such as HCl and NaOH affects proteins. It was observed that different denaturants act upon or denature protein differently. This was determined using the principle of viscometry. An Ostwald viscometer was used to measure the viscosity of the prepared native‚ blank‚ denatured native and blank with denaturant solutions. The time required for the said solutions to pass through the viscometer
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The Isolation‚ purification and identification of Proteins assayed From Bovine Liver Using SDS Gel Electrophoresis‚ Mass Spectroscopy and Western Blotting Abstract The purpose of the experiment was to isolate and recognize varying protein solubilization and assaying methods by using bovine liver protein. The experiment implicated the impact of different types of solvents like ethanol‚ water‚ PBS‚ PBS+1% Triton x-100‚ and PBS+2% SDS on protein solubilization. Bradford and Ghosh/Dumbroff methods
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DENATURATION OF PROTEINS Abstract The experiment aimed to use the concept of viscosity to study the effects of different denaturants on 1% albumin extract. An Ostwald viscometer was used to measure the flow time of 5 mL of the blank and native protein. These were then denatured by adding 1 mL of denaturant and had their flow time measured. The flow time from the blank to denatured protein is increasing. The specific viscosity and reduced viscosity
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4A.2 RRL 4A.2.1 Coagulation of Proteins Coagulation of protein refers to sticking together‚ like a blood clot‚ usually as a result of denaturation or coming out of solution due to abnormal ionic strength or a change of solvent. Definite characteristics of the proteins are changed when they are coagulated‚ among which is loss of solubility in water and dilute salt solutions. In some instances and under certain conditions the coagulation process may be reversible. (Campbell‚ et.al‚ 1979) 4A.2.2
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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 the protein concentration
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Title: Determination of Iron in Natural water by Spectrophotometry. Aim: To determine the iron in natural water by spectrophotometry. Abstract: The iron in natural water was determined by utilizing spectrophotometric analysis. That was done by measuring the absorbance of five Fe(oPH)2+3 standards at 510 nm. From that information‚ a calibration curve was plotted and used to find the amount of Fe2+ that was in two unknown water samples based on the absorbance readings obtained with them at 510nm. The
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Discovered in 1838‚ proteins are recognized as a large number of superior organic compounds that make up living organisms and are essential for their functioning. In other words proteins are the building blocks of life. They do many tasks for the human body and other organisms‚ that could not be done individually. These macromolecules could function as structural proteins and form structures such as keratin in hair‚ teeth‚ bones‚ muscles‚ collagen in connective tissues‚ horns in animals
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Introduction: Protein texturization is a process of protein transform from a globular state to a fibrous physical structure that contains a sensation of eating meat. Texturized protein products have been defined as “fabricated palatable food ingredients processed from an edible protein source including among other soy grits‚ soy protein isolates and soy protein concentrate with or without suitable option ingredients added for nutritional or technological purposes.” (R.Y Yada‚ 2004) Protein products that
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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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determine the Keq of the formation of Fe(SCN)2+ through the use of UV-Vis spectrophotometry. The solutions used in the study were allowed to equilibrate days before calibration in a UV-Vis spectrophotometer which determined the absorbance and thus the molar absorptivity of Fe(SCN)2‚ which was found to be 1.942 x 10-3 M-1cm-1. Given the molar absorptivity and absorbance‚ Beer-Lambert’s Law gave the equilibrium concentrations for the product and reactants and from that‚ the Keq of the formation of Fe(SCN)2+
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