Violet ring at the junction where the two layers meet | Absence of purple ring | * Acid hydrolysis is a better procedure than Alkaline hydrolysis because of the less destruction of amino acids Experiment 3: Protein Assay by Bradford Method * Coomassie Brilliant Blue G-250 * Bradford Reagent * Bovine Serum Albumin = BSA * Reagent blank = test tube #1 = 0mL BSA stock solution‚ 1mL distilled H2O * 595nm * Plot A595 vs concentration of BSA Experiment 4: Enzymatic Activity of Salivary
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Genetic Transformation of Bacteria Abstract The transformation of bacteria was successfully carried out using a plasmid carrying a gene that codes for green fluorescent protein‚ which gives a signature green glow reminiscent of a jellyfish. This gene‚ however‚ is only active when the sugar arabinose is present. A gene coding for antibiotic resistance was also found within the plasmid and served as a means to verify that transformation had indeed taken place. The hypothesis was that the bacteria
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Fish phylogenetic tree based on protein size Amanda Reed Lab partners: Lecia Redwine‚ Kyle Hatcher TA: Baneshwar Singh Biology 117‚ Section 25 Tuesday 10:30 AM Introduction Although tree diagrams have been used since the days of Charles Darwin‚ biologists have only recently adopted the tree model of evolution to read and interpret phylogenies. One of the reasons for this is the confusion that often arises from using a tree model to describe a phylogeny (Baum‚ 2008a). Many people interpret
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Western Blotting is used to Identify a Subunit of Myosin Light Chain in the Proteins of All the Different Fish. Chae Yee Kent State University: BSCI 30140 Lab Abstract Western Blotting can be used to detect the Myosin actin light chain in different species of fish and is used to distinguish from different species based on variation‚ commonality‚ or evolutionary divergence. First‚ proteins are extracted from the tissue and loaded into a gel matrix. The matrix will separate the proteins according
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Materials and Methods Growing the G Strain and Preparing the GCE (rGFP Crude Extract): To grow the bacterial culture‚ use 10 ml of liquid LB growth media for incubation. 500 ml of the bacterial culture is allowed to grow overnight at 37°C. It is later shaken vigorously to increase the OD600 to 0.5‚ which means that time equals zero. At time zero‚ 1 mL of the culture is transferred into a 1.5 mL centrifuge tube and centrifuged for 5-10 minutes to obtain a pellet. The supernatant should be discarded
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DEVELOPING A CONVENIENT ANALYTICAL TECHNIQUE FOR THE QUANTITATIVE ESTIMATION OF RESIDUAL CTAB PRESENT IN HEAMOPHILUS INFUENZAE type b POLYSACCHARIDE Thesis submitted for the degree of Bachelor of Technology Biotechnology 1 BY 2 Mr. Sarthak Ranka 2 Under the guidance of 1 Dr. SURESH BERI ADDITIONAL DIRECTOR (PRODUCTION) Serum Institute Of India Ltd 212/2‚ Hadapsar Pune (MH)-411028 1 Submitted to
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h at 4C using a Beckman Coulter’s TLA 100 rotor. At stop‚ the top 80 µL was considered as supernatant (S) and the remaining 20 µL added with 60 µL (Buffer A) as pellet (P). Thus obtained volumes were analyzed on a 10% SDS-PAGE and stained using Coomassie blue for quantification by Image J (National Institutes of Health‚ MD). Compensating the dilution of the pellet‚ the true Intensity of the pellet will be‚ IPellet = Ip – 0.25xIS‚ while IP & IS being experimental values obtained for pellet and supernatant
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The Kinetics of α-Chymotrypsin Introduction Chymotrypsin is a protease which cleaves proteins by a hydrolysis reaction‚ it does this by adding a molecule of water to a peptide bond. Although the hydrolysis reaction is thermodynamically favoured in the absence of a catalyst the half-life for a typical hydrolysis reaction by a protease is between 10 and 100 years‚ needless to say it is extremely slow1. Though this is true peptide bonds are hydrolysed within milliseconds in the body in the presence
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Separation of Proteins and Mass Analysis Using SDS PAGE Biology 00-01L Abstract This experiment consisted of separating proteins into polypeptides using a method called SDS PAGE which is a type of electrophoresis. The polypeptides had different masses‚ so each polypeptide traveled a different distance and this was an essential part of the lab which demonstrated that there exists a relationship between the distance traveled by the protein and the mass of the protein. This relationship was graphed
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Objective: The main objective for this lab was to use the Bradford and DC Protein Assay in order to determine our concentration of E. Coli BL21(DE3) lysate. Principle of Methods: To accomplish this objective‚ each pair of lab partners received an E. Coli lysate sample which we had to thaw by warming it with our hands and centrifuge it. We extracted a total of 12 samples with known concentrations of bovine serum albumin and 10 samples of different amounts of lysate put into them. Using the different
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