Expression of a functional recombinant fusion protein via the directional sub-cloning of an E.coli derived tyrosine phosphatase gene (wzb) into a pT5(6H)CFP mutant expression vector. Abstract: Application of fluorescent fusion proteins to the field of expression and interaction proteomics as a means of dynamic imaging proteins in vivo has allowed for rapid advancements in biotechnology research. Production of such proteins first involves the insertion of a given protein-coding gene transcriptionally
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investigate the effect of different alkaline solution on the quality of yellow wet noodles. There were four different formulations that we used. According to the table A in the procedure‚ it stated that for formulation 1‚ we were using Sodium Carbonate with sodium chloride as the alkaline salt solution while formulation 2 with Soda Ash with sodium chloride and formulation 3 with Potassium Carbonate with sodium chloride . However for formulation 4‚ we were not using any alkaline solution to make it become
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Germination of Eggplant (Solanum melongena Linn.)‚ Okra (Abelmoschus esculentus (L.) Moench)‚ and Rice (Oryza sativa Linn.) Seeds Soaked in Alkaline Water In Partial Fulfillment of the Requirements In Bi 160 and Bi 160.1 First Semester‚ AY 2012-2013 A Research Paper Presented to Anneke Padolina‚ Ph.D Department of Biology Ateneo de Manila University Submitted by: Medina‚ Kryzka August 2012 I. Introduction The life cycle of plants is characterized by the change in ploidy
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Edinburgh and while attending school he began his experiments. He obtained his medical degree in 1754. After graduation‚ Black continued his experiments and kept a journal of all his experiments. “Experiments Upon Magnesia Alba‚ Quicklime‚ and some other Alkaline Substances‚” was written by Joseph Black‚ MD. The journal detailed his experiments with Magnesia Alba. “The Life and Letters of Joseph Black: Chapter
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Chemistry Practical Report: Period 3 Elements Name: Titus Lee Date: 12th February 2014 Partners: Louella Jarillas‚ Vevaan Nguyen‚ Alexandro Francisco‚ Alif Ahmed Aim: To examine the similarities and differences between the properties of a selection of the elements of Period 3 Hypothesis: Sodium will be the most reactive element and sulphur will be the least reactive Equipment and Method: Found on Page 28-9 in Heinemann Chemistry 1 Student Workbook Results: Element Observations Element
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reaction is considered where a colorless Paranitrophenol Phosphate (PNPP) is converted to the yellow paranitrophenol (PNP) through the action of an enzyme called alkaline phosphatase. This enzyme normally acts on molecules that have a phosphate group by cleaving it. The main purpose of the experiment is to study the kinetics of alkaline phosphatase when acting on a conversion of PNPP to PNP by measuring the activity of the enzyme in terms of the amount of the product made. Since PNP has a yellow color
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of the reaction. Alkaline phosphatase is made throughout the body. Its function is to remove phosphate groups from nucleotides and proteins‚ many enzymes have their activity controlled by the addition and removal of phosphate groups. The blood serum level of Alkaline
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REFERENCE ID: 201002578 TITLE SCREENING PREGNANT WOMEN FOR PERIODONTITIS BY ANALYSING SALIVARY ALKALINE PHOSPHATASE AND LACTATE DEHYDROGENASE INTRODUCTION Periodontal disease can induce systemic inflammatory and immune responses and may be associated with an increased risk of systemic diseases such as cardiovascular disease and rheumatoid arthritis.1–3 Periodontal disease is common in pregnant women4 and increases the risk of adverse pregnancy outcomes including preterm birth‚ low birth weight
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words count: 1‚313 Determination of Km and Vmax of Alkaline Phosphatase Graphs will be used with the enzyme alkaline phosphatase of the unknown in the enzyme solution to Determine Km and Vmax To Dr. Kimberly A. P. Mitchell‚ Editor‚ Liberty Journal of Cell Biology‚ 1971 University Blvd‚ Lynchburg‚ VA 24502. Materials and Methods Dilution: Alkaline Phosphatase The objective of this laboratory is to determine the velocity of alkaline phosphatase and make a graph of rate vs substrate concentration
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INTRODUCTION Alkaline phosphatase catalyses the hudrolysis of p-nitrophenyl phosphate (a synthetic substrate) at an optimum pH of 10.0 with the liberation of p-nitrophenol. The substrate is colourless‚ but the product p-nitrophenol is yellow in alkaline solution‚ absorbing maximally at 405 nrn. Thus a convenient assay for this enzyme involves monitoring the change in absorbance of the reaction medium at 405 nm. Exergonic (i.e energy producing reactions) exhibit a negative free energy change
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