the function of glucose used in conjuction with lysozyme in isolation of plasmid DNa?
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This seems like a hard question but if I understand it right it is asking you why glucose is used in isolation of plasmid DNA.  From my deduction it is simply a growth medium for the bacteria providing enough bacteria with the plasmid.  Then the lysozyme is added to break down the cell walls of the bacteria to begin the isolation of plasmid DNA.  This source may help: http://www.bio.com/protocolstools/protocol.jhtml?id=p571
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The phenotype is the physical expression of the genotype. In bacteria transformed with the pBLU plasmid and plated on the growth media containing IPTG and X-Gal will grow as either white colonies or blue colonies. pBLU is a plasmid that contains part of a gene called beta-galactosidase. The portion of the plasmid that contains this gene is called the multiple cloning site (MCS). (If you want to introduce foreign DNA into the plasmid, this is where you would introduce it.) The plasmid also has a gene for antibiotic resistance. The bacteria you use for transform with this plasmid must not already have this type of antibiotic resistance. If the bacteria are transformed with pBLU and plated on media with anibiotics only the bacteria that recieved the plasmid will grow. Those that were not transformed will die. If no DNA was inserted into the MCS of the plasmid then the for producing beta-galactosidase will be intact. This gene is called Lac Z. The transcription of this gene must be induced with a chemical called IPTG. So if the agar plate contained IPTG then the Lac Z gene will be induced and the protein beta-galactosidase will be produced. If this protein is produced it will cleave the chemical X-Gal (which was also on the plate) causing the X-gal to change from clear to blue.This causes the colonies to have a blue phenotype.\nIf the Lac Z gene was interrupted by foreign DNA in the MCS then no beta-galactosidase will be produced and the colonies will grow white.
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(I just did this today in lab with bacteria instead of onions!) Other liquids can do many things to DNA, but water binds to the DNA and "elutes" it, the DNA will stay with the water. (look up "elute")
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most likely a starch molcule, which is just a simple polymer of glucose, if the enzymes from the yeast extract were intact.
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How is Recombinant DNA made? \nThere are three different methods by which Recombinant DNA is made. They are \nTransformation, Phage Introduction, and Non-Bacterial Transformation. Each \nare described separately below. \n\nTransformation\nThe first step in transformation is to select a piece of DNA to be inserted \ninto a vector. The second step is to cut that piece of DNA with a restriction \nenzyme and then ligate the DNA insert into the vector with DNA Ligase. The insert contains a selectable \nmarker which allows for identification of recombinant molecules. An antibiotic \nmarker is often used so a host cell without a vector dies when exposed to a certain \nantibiotic, and the host with the vector will live because it is resistant. \n\nThe vector is inserted into a host cell, in a process called transformation. One \nexample of a possible host cell is E. Coli. The host cells must be specially \nprepared to take up the foreign DNA. \n\nSelectable markers can be for antibiotic resistance, color changes, or any other \ncharacteristic which can distinguish transformed hosts from untransformed hosts. \nDifferent vectors have different properties to make them suitable to different \napplications. Some properties can include symmetrical cloning sites, size, and \nhigh copy number. \n\nNon-Bacterial Transformation\nThis is a process very similar to Transformation, which was described above. The \nonly difference between the two is non-bacterial does not use bacteria such as E. Coli \nfor the host. \n\nIn microinjection, the DNA is injected directly into the nucleus of the cell being \ntransformed. In biolistics, the host cells are bombarded with high velocity \nmicroprojectiles, such as particles of gold or tungsten that have been coated \nwith DNA. \n\nPhage Introduction\nPhage introduction is the process of transfection, which is equivalent to transformation, \nexcept a phage is used instead of bacteria. In vitro packagings of a vector is used. \nThis uses lambda or MI3 phages to produce phage plaques which contain recombinants. \nThe recombinants that are created can be identified by differences in the \nrecombinants and non-recombinants using various selection methods.
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I think you might be refering to plasmids.\nA plasmid is a small circular piece of DNA found in bacteria. A plasmid will often include genes which encode a protein that confers resistance to antibiotics. They can be transferred fromn one bacterium to another and replicate separately from the bacterial genomic DNA. One bacterium can contain many copies of a particular plasmid.\n\nLook it up & see if it is relevant to your enquiry.
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Check this out: \nhttp://www.phschool.com/science/biology_place/biocoach/lacoperon/lactose.html\n\nhttp://www.mun.ca/biochem/courses/4103/topics/lac_operon.html
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In order to perform in vitro analyses, a protein must be purified away from other cellular components. This process usually begins with cell lysis, in which a cell's membrane is disrupted and its internal contents released into a solution known as a crude lysate. The resulting mixture can be purified using ultracentrifugation, which fractionates the various cellular components into fractions containing soluble proteins; membrane lipids and proteins; cellular organelles, and nucleic acids. Precipitation by a method known as salting out can concentrate the proteins from this lysate. Various types of chromatography are then used to isolate the protein or proteins of interest based on properties such as molecular weight, net charge and binding affinity. The level of purification can be monitored using gel electrophoresis if the desired protein's molecular weight is known, by spectroscopy if the protein has distinguishable spectroscopic features, or by enzyme assays if the protein has enzymatic activity.\n\nFor natural proteins, a series of purification steps may be necessary to obtain protein sufficiently pure for laboratory applications. To simplify this process, genetic engineering is often used to add chemical features to proteins that make them easier to purify without affecting their structure or activity. Here, a "tag" consisting of a specific amino acid sequence, often a series of histidine residues (a "His-tag"), is attached to one terminus of the protein. As a result, when the lysate is passed over a chromatography column containing nickel, the histidine residues ligate the nickel and attach to the column while the untagged components of the lysate pass unimpeded.\n\n\n[edit] Cellular localization\n \nProteins in different cellular compartments and structures tagged with green fluorescent protein.The study of proteins in vivo is often concerned with the synthesis and localization of the protein within the cell. Although many intracellular proteins are synthesized in the cytoplasm and membrane-bound or secreted proteins in the endoplasmic reticulum, the specifics of how proteins are targeted to specific organelles or cellular structures is often unclear. A useful technique for assessing cellular localization uses genetic engineering to express in a cell a fusion protein or chimera consisting of the natural protein of interest linked to a "reporter" such as green fluorescent protein (GFP). The fused protein's position within the cell can be cleanly and efficiently visualized using microscopy, as shown in the figure opposite.\n\nThrough another genetic engineering application known as site-directed mutagenesis, researchers can alter the protein sequence and hence its structure, cellular localization, and susceptibility to regulation, which can be followed in vivo by GFP tagging or in vitro by enzyme kinetics and binding studies.\n\n\n[edit] Proteomics and bioinformatics\nMain articles: Proteomics and Bioinformatics\nThe total complement of proteins present in a cell or cell type is known as its proteome, and the study of such large-scale data sets defines the field of proteomics, named by analogy to the related field of genomics. Key experimental techniques in proteomics include protein microarrays, which allow the detection of the relative levels of a large number of proteins present in a cell, and two-hybrid screening, which allows the systematic exploration of protein-protein interactions. The total complement of biologically possible such interactions is known as the interactome. A systematic attempt to determine the structures of proteins representing every possible fold is known as structural genomics.\n\nThe large amount of genomic and proteomic data available for a variety of organisms, including the human genome, allows researchers to efficiently identify homologous proteins in distantly related organisms by sequence alignment. Sequence profiling tools can perform more speci
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Restriction enzymes are cutting enzymes found in bacteria. They cut within the DNA molecule and are called restriction endonucleases. They recognize a specific sequence 0f DNA nucleotides and cut the molecules there, producing sticky ends. A missing gene is then added. Another enzyme, DNA ligase, attaches back the DNA molecule. So, of course you end up with two DNA strands. The new DNA produced is known as recombinant DNA. This technology is used in human therapy. Some examples are: human insulin to treat diabetes type I and human factor VIII for the treatment of hemophilia.
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Restriction enzymes, also called restriction nucleases (EcoRI in this example) , surrounds the DNA molecule at the point it seeks(sequence GAATTC). It cuts one strand of the DNA double helix at one point and the second strand at a different, complementary point (between the G and the A base). The separated pieces have single stranded "sticky-ends," which allow the complementary pieces to combine. \n\nThe newly joined pieces are stabilized by DNA ligase.\n\nEcoRI, one of many restriction enzymes, is obtained from the bacteria Escherichia coli.
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DNA Technology\nRecombinant DNA technology refers to the techniques used to transplant genes from one living source into another where it will be expressed.\n \nHow Does it work?:\nThe science of DNA technology includes the use of special enzymes called restriction enzymes, DNA vectors, and the host organisms. We will take a look at each of these groups in the following section.\n \nRestriction Enzymes:\nThese special enzymes were discovered in the late 1960's as naturally occurring agents in bacteria. They protect the bacterium against foreign DNA from other organisms. Invading DNA is cut into pieces and made inoperable. This process is called restriction. As with any enzyme, these are specific in the job they do. Many of them only recognize short, specific nucleotide sequences( recognition sequences) and cut at specific points within those sequences. Bacteria protect their own DNA by a process called methylation. During this process methyl groups are added to the nucleotides within the recognition sequence. There are several hundred restriction enzymes and about 100 different recognition sequences.\nRecognition Sequences: are symmetric in that the same sequence of 4 to 8 nucleotides is found on both strands, but run in opposite directions. The restriction enzymes usually cut the phosphodiester bonds of both strands in a staggered manner. The result being both ends have a single stranded area called the sticky ends. It is within this space that the new piece of DNA is added, attaching to the sticky ends. \n \nThese unions are temporary until the enzyme DNA ligase is added to catalyze the formation of the phosphodiester bonds.\nVectors: are used as carriers for moving DNA from test tubes into cells. Bacterial plasmids and viruses are the most widely used vectors in DNA transfer. Bacterial cells can pick up the DNA through the process of transformation. Lambda phages are used by eliminating the middle of its liner genome and adding the foreign DNA in the created space. The phage is then introduced into the bacterial cell where it replicated itself via the lysogenic cycle.\nHost Organisms: Bacteria are usually used as hosts in genetic engineering. There are several reasons why they are chosen. 1. Bacterial DNA can be easily isolated and reintroduced into bacterial cells. 2. Bacterial cultures grow quickly. Some disadvantages surface as well: 1. Bacteria, being prokaryotic, may not be able to use the information in eukaryotic genes. 2. Bacterial cells cannot make the the necessary changes in transcription to produce some eukaryotic proteins. Eukaryotic cells can also be used as hosts. Yeast cells and some plant and animal cells can be a host for foreign DNA, but it is often difficult to get such cells to take up engineered DNA.\nSteps for using Bacteria and Plasmids to Clone Genes:\n1. Isolation of two kinds of DNA.\n2. Treatment of plasmid and foreign DNA with the same restriction enzyme.\n3. Mixture of foreign DNA with clipped plasmids.\n4. Addition of DNA ligase.\n5. Introduction of recombinant plasmid into bacterial cells.\n6. Production of multiple gene copies by gene cloning and selection process for transformed cells.\n7. Final screening for transformed cells.\n \n\n \nAdditional Methods for Analyzing and Cloning Nucleotide Sequences:\n1. Gel Electrophoresis. is used to separate either nucleic acids or proteins based upon molecular size, charge and other physical properties. Various DNA's can be identified by their characteristic banding patterns after being cut with their particular retraction enzymes. Genes can be isolated, purified and recovered from the gel with full biological activity.\n2. DNA Synthesis. It is possible to create known short DNA sequences in the laboratory. The Sanger Method is used to identify the sequence of a DNA molecule. This method is based on: a). use of restriction enzymes into small reproducible fragments. b). produce in a test tube DNA strands complimentary to a strand from the restr
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In 1869 Friedrich Miescher, a Swiss researcher, stained a cell nucleus with bromine I think, and found that something in it would stain.  He extracted this something and determined that It was composed of phosphoric acid, nitrogenated organic bases and sugar.\n\nIn 1943 Oswald Avery, a Canadian researcher found that bacteria would transform when washed, when exposed to protease, but not when exposed to deoxyribonuclease.  This led him to conclude that the something Miescher found was by composition supposed to be called deoxyrybonucleic acid and that this DNA was in fact the basic unit of heredity because doexyribonuclease is an enzyme that eats up DNA.\n\nThat's the evidence.\n\nOut genomes aren't made of RNA because that is a single stranded chain. Nothing wrong with that, but it's less sturdy than DNA, which is double stranded and supercoiled and so on.  It's a matter of what is the better means of storing your genetic information.
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The purpose of adding salts is to neutralize the charge on the sugar-phosphate backbone of the DNA, but ethanol's task is a little more complex than "removing" the water. For a precipitation, you're interested in forming ion pairs between the polyanion (DNA) and the cation (Na+, Mg++, spermidine, protamine, etc). In dilute aqueous solution, DNA and counterions like Na+ and Mg++ are more or less in the free ion form rather than the ion pair form (that is, they are surrounded by one or more layers of water molecules).\n\nWater has a high dielectric constant (e), which from Coulomb's Law tells us that the electrostatic force (F) between two ions of opposite charge is very low in water:\n\nF = (Q1 * Q2)/(e * r2)\n\nwhere Q is the charge on each ion and r is the distance between them. Adding organic solvent(read ETHANOL) *decreases* the dielectric constant of the solution. As e goes down, F goes up and *BANG*, anion and cation form an ion pair and promptly swoon out of solution.
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Differences\n1.Cellulose is a carbohydrate useful for giving streght to cell wall in planta and bacteria\n1.Dna is the genetic material which determines the characters of ofsprings.\n\n2.Cellulose is made up of  glucose -a poly mer of glucose, homopolymer\n2.dna is a polymer of four nucleotide-heteropolymer\n\n3.cellulose is branched polymer\n3.dna is unbranched\nthis are the few diferences.
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When the two glucose molecules join, two hydrogen and one oxygen atoms are released, so I think the answer to your question is that the larger molecule is the maltose and the smaller is water (H2O).\n\nHope this helps - now get on with your homework!!  ;-)
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do you mean interactions BETWEEN nucleic acids and proteins?  If so there's a lot of ways you can study that - you can do a footprint analysis - digest the nucleic acid in the presence of the protein and see what piece gets protected to see where the protein binds if you know the identity of the two interacting molecules.  If you don't know their identity you can try a gel-shift assay where DNA will move at different rates on a gel in the presence and absence of various proteins.  If you know the protein but not the DNA you can try an affinity column with the protein immobilized and then try to determine which DNA sequences bind.  You can also try to determine the crystal structure of a co-crystal if you have a lot of the two materials.  good luck!
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http://www-sequence.stanford.edu/group/techdev/plasmid.html