what is the application of totipotency in tissue culture?
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Totipotent cels are cells that haven't started differentiating.  The idea is that you could use them to replace cells in the body that are otherwise irreplaceable, like nerve cells.  All you have to do is subject a totipotent cell to the chemical cascade that triggers them to differentiate into the desired cell.  Replaceable cells (like epithelial cells) do this in your body all the time, but they start from pluripotent stem cells, which can become any of a finite number of different cells types.  But a totipotent cell can turn into any cell at all, given the proper developmental signals.
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You've asked a rather broad question.\n\nHere's a good place to start:\n\nhttp://en.wikipedia.org/wiki/Kingdom_%28biology%29\n\nMore specific questions would be easier to answer.
922145
A. TPP is an important cofactor generally needed for decarboxylases
82949
To trigger a biological response.
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Abstract. \n...membranes, microvilli, and membrane projections, and act as crosslinkers between the actin cytoskeleton and proteins of the cell surface...\nhttp://147.52.72.117/IJO/2002/volume21/number5/935-940.pdf \n\n \nforthcoming meetings\nAim: to learn techniques commonly used to analyse signal transduction ... and cell adhesion (cytoskeleton, cell adhesion proteins, extracellular\nhttp://www.usgeb.ch/skmb2005.html \n\n \nBTO\n...and function of proteins, methods of ... Cytoskeleton and cell motility. ... Describe and use structure determination techniques to analyse\nhttp://www.bto.ed.ac.uk/courses/year1/index0506.phtml \n\n \nRandall Division o f Cell and Molecular Biophysics\n...actin cytoskeleton during migration. I use a number of different advanced imaging techniques to analyse ... analysis of interacting proteins by\nhttp://www.kcl.ac.uk/depsta/biomedical/randall/mparsons.html \n\n \nGlossaire (ULg)\nAnkyrins. A family of membrane-associated proteins responsible for the attachment of the cytoskeleton. Note: membrane proteins \nhttp://www.ebm.lib.ulg.ac.be/prostate/gloss.htm \n\n \nThe role of the axolemma in the initiation of traumatically induced...\n...proteins. Transmembrane proteins such ... matrix to the cytoskeleton via the ... Biophysical investigations have used novel techniques to\nhttp://www.jnnp.com/cgi/content/full/64/3/285 \n\n \nThe tiniest parts of \n...are as dispart as the techniques and ... natural science, is to analyse the ... energy or information, signal transducers, cytoskeleton...\nhttp://www.uni-leipzig.de/~philos/psarros/preprints/the_tiniest_parts_of.html \n\n \nGenome Biology | Full text | Analysis and functional classification\n...as well as the development of new techniques for ... genes encoding cytoskeleton proteins (such as myosin, actin, UNC-87, troponin T) and\nhttp://genomebiology.com/2003/4/4/R26 \n\n \nStudy Abroad 2004 INTRODUCTION 2 Deakin University's unique Study \nUnit Handbook GUIDE TO UNIT DESCRIPTIONS ACD206/306 Dance Production and Analysis Second semester, 1 credit point Prerequisite ACD203 or Level One \nhttp://www.deakin.edu.au/international/Documents/Brochures/SAHandbook.pdf \n\n \nAdrian Harwood\n...genetic, biochemical and cell biological techniques to analyse the ... has both a cytoskeleton and a network ... SH2 domain proteins,\nhttp://www.ucl.ac.uk/LMCB/pages/harwood.html
182868
Depends on the cell type labile, stable, non regenerative etc
463857
well it depend on the species of animal or plant you're studying. in Mammalian cells, The protein mTOR is a serine/threonine kinase that regulates DNA translation and cell division. the availability of a food source for the cell influences mTOR so that when cells are not able to grow to normal size they will not go through cell division. This is just one of the proteins synthesized during different times of a cell cycle to prevent mitosis from occuring. some disrupt the formation of mitotic spindles, some prohibit the cell from going into prophase or metaphase...others work on chemical receptors and hormones released form the cell. google search it, and I hope this has helped :)
294304
Interferes with the peptidogylcan layer of the cell wall. Causes cell to be prone to lysis. (Bursting)\n\nWhat I usually do is use google to search for relevant sites. Wikipedia is another great resource with easy to understand information. http://wikipedia.com \n\nHere are some more regarding your question\nhttp://helios.bto.ed.ac.uk/bto/microbes/penicill.htm\nhttp://www.cat.cc.md.us/courses/bio141/lecguide/unit1/prostruct/penres.html\nhttp://mic.sgmjournals.org/\nhttp://www.microbes.info/\nhttp://www.bact.wisc.edu/Microtextbook/\nhttp://www.microbiol.org/\nhttp://www.asm.org/
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Plasma-derived serum as a selective agent to obtain endothelial cultures from swine aorta.\n\n\n\nEndothelial cell and smooth muscle cell cultures from artery wall provide a potential model system for studying cellular processes involved in atherogenesis. To prepare serial subcultures of swine arterial endothelial cells that are free of smooth muscle cells without either selecting a small population or subjecting the cells to cytotoxic conditions, we used swine plasma-derived serum (SPDS) to establish conditions in which endothelial cells have a growth advantage. Endothelial cells were collected by collagenase digestion and smooth muscle cell cultures were prepared by outgrowth from explants of arterial medial segments. Growth rates were compared when each cell type was maintained on SPDS, or fetal bovine serum (FBS), or swine whole serum (SWS). When 20% FBS or SWS were used the doubling times were less than 30 h for both endothelial cells and smooth muscle cells. On 20% SPDS the doubling time for endothelial cells was 32 h, but for smooth muscle cells it was at least 168 h. Using SPDS, we prepare endothelial subcultures from swine aorta that express principally polygonal morphology at confluence. Endothelial cell cultures grown on SPDS have higher angiotensin-converting enzyme than those grown on FBS.\n\nBlood and serum are frequently used as samples for proteomic analysis. A consideration of the literature suggests that the differences between serum and plasma as samples are not appreciated by many investigators. There also appears to be a lack of understanding of the issues critical for the processing of plasma and serum samples for analysis. The major difference between plasma and serum is the removal of fibrinogen and associated proteins such as high-molecular weight von Willebrand factor and the variable addition of cellular secretion products as a result of the coagulation process. Factors influencing plasma quality include anticoagulant selection, processing, and storage. Factors influencing serum quality include collection container and clot retraction time. Various approaches for the removal of high abundance proteins such as albumin and immunoglobulin G will be discussed. While it is clear that the removal of these high abundance proteins provides for the analysis of otherwise obscured low-abundance proteins, studies have not been performed to document that some low-abundance proteins are also not removed by these techniques Furthermore, most studies do not have enough "normal" subjects to provide a statistically sound control value. Plasma and serum can be valuable samples for proteomic analysis but the preparation of the samples must be suitable for regulatory validation. Recommendations are presented for consideration.\n\nDoes this help?
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ALl of the above is true BUT..plasmids with appropriate selectional markers CAN be transfected into cells (mainly cell or tissue culture) so that they contain plasmids.  So long as the selectional pressure is maintained, the plasmid will remain there.
557413
(m)\n\nThe coleoptiles of grasses (like that of oat, the Avena - coleoptile) are popular test objects of plant physiology. A growing coleoptile that is illuminated unilaterally does grow towards the light source. This behaviour is common among plants and is known as phototropism. C. DARWIN (assisted by his son Francis DARWIN) attributed in his work "The Power of Movement in Plants" (1880) a decisive function in the recognition of a light stimulus to the coleoptile’s tip, and he observed that the actual bending occurs in a zone below the tip. He concluded that a transmission of impulse had to take place in the tissue. Studies of plant anatomical nature revealed that the growth towards light is caused by an elongation of the cells at the side that is shielded from the light. The phototropic reaction does not happen if the coleoptile’s tip is removed, though it can be induced again by the replacement of the tip. This indicates the existence of a substance that is spread from tip to bottom (basipetal direction) and that causes the elongation. \n\nThe Danish botanist P. BOYSEN-JENSEN interrupted the assumed substance flow by inserting a mica sheet into the shielded side thus separating the coleoptile’s tip from the tissue below (1913). The water-impermeable sheet interrupted the phototropic reaction. Consequently occurs no transport of the effector around the small tile. The phototropic reaction remained intact when the mica sheet was inserted into the illuminated side or along the coleoptile’s vertical axis. \n\nIn the late twenties was the material nature of the effector finally proved by the Dutch plant physiologist F. WENT. He assumed that a substance that flows from tip to bottom should also flow through a small cube of agar. In order to test his assumption did he place cut coleoptile tips with the cutting side on top of small cubes of agar. Some time later did he remove the tips and placed the agar cubes that he believed to contain the effector onto the decapitated coleoptiles
942751
Sorry for my previous answer, I was mistaken. \nI believe answer is B. A is correct, but I don't think it is why it affect target tissue for loger time. I don't think C is correct, but it could be. D is certainly wrong and E too. I haven't seen this in a while. Sorry I couldn't be more help.
280288
Firstly, protoplasts are naked cells without cell walls. Protoplast regeneration is a method for obtaining whole plants from protoplasts.\n\nThere are 2 ways used to release protoplasts from plant tissue. 1. mechanical dissection or rupture of the cell walls ; or 2. the more common method involving enzymes that digest the cell wall.\n\nThe protoplasts are embedded in alginate -- a medium containing nutrients, organic acids, vitamins, and high concentrations of different sugars to stabilize the naked protoplasts until the cell walls reformed. Ultimately, each protoplast will develop into a callus of tissue that can then be induced to differentiate to produce a new plant (a clone of the original plant). This method can produce way more new plants than the traditional propagation methods.
214979
You can check out this site, it explains a step by step technique:\n\nhttp://www.pall.com/biosepra/34696_7290.asp
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(m)\n\nCloning of Plant Cells and Manipulation of Plant Genes\nPlant cells exhibit a variety of characteristics that distinguish them from animal cells. These characteristics include the presence of a large central vacuole and a cell wall, and the absence of entioles, which play a role in mitosis, meiosis, and cell division. Along with these physical differences, another factor distinguishes plant cells from animal cells, which is of great significance to the scientist interested in biotechnology: Many varieties of full-grown adult plants can regenerate from single, modified plant cells called protoplasts - plant cells whose cell walls have been removed by enzymatic digestion. More specifically, when some species of plant cells are subjected to the removal of the cell wall by enzymatic treatment, they respond by synthesizing a new cell wall and eventually undergoing a series of cell divisions and developmental processes that result in the formation of a new adult plant. That adult plant can be said to have been cloned from a single cell of a parent plant. \nPlants that can be cloned with relative ease include carrots, tomatoes, potatoes, petunias, and cabbage, to name only a few. The capability to grow a whole plant from a single cell means that researchers can engage in the genetic manipulation of the cell, let the cell develop into a completely mature plant, and examine the whole spectrum of physical and growth effects of the genetic manipulation within a relatively short period of time. Such a process is far more straightforward than the parallel process in animal cells, which cannot be cloned into full-grown adults. Therefore, the results of any genetic manipulation are usually easier to examine in plants than in animals.
745545
these might help..\n\nhttp://www.blackwell-synergy.com/doi/abs/10.1111/j.1365-2621.2006.01347.x\n\nhttp://www.co-lipidology.com/pt/re/colipidology/abstract.00041433-200502000-00009.htm;jsessionid=Fh8fr0yV02g1pkF1LGYLXyzy9lPXZ4Gn69QZKHJ1GG1vJYGw1czy!-1640309041!-949856145!8091!-1\n\nhttp://scholar.google.com/scholar?hl=en&lr=&q=cache:yYCPrA4fU54J:bmc.ub.uni-potsdam.de/cgi-bin/show.pl%3F1475-2891-4-33/1475-2891-4-33.pdf+list+of++biochem+experiments,+TEAC+assay+or+the+phenolics+test
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The Lowry Method\nThe Lowry method for determining protein concentration\nis essentially a biuret reaction that incorporates\nthe use of Folin-Ciocalteu reagent for\nenhanced color development. The Lowry procedure\nis more commonly used in research applications\nbecause it is ten times more sensitive than\nthe biuret reaction. In the Lowry method, protein is\nfirst treated with alkaline copper sulfate in the\npresence of tartrate. This “incubation” is then followed\nby addition of the Folin-phenol reagent. It is\nbelieved that the enhancement of the color reaction\nin the Lowry procedure occurs when the tetradentate\ncopper complexes transfer electrons to the\nphospho-molybdic/phosphotungstic acid complex\n(Mo+6/W+6, Folin phenol reagent). Reduction of the\nFolin phenol reagent yields a blue color read at 750\nnm.17,18\nAlthough the Lowry method has the distinction of\nbeing the most referenced assay in the biochemical\nliterature and has become the standard for protein\nquantitation, it is also well known for its deficiencies.\nFor example, the alkaline copper reagent\nis unstable and requires daily preparation with a\nmulti-step procedure that is time- and labor-intensive.\nIn addition, the assay has been shown to be\nphotosensitive. As a practical matter, precautions\nReferences\n4. Peterson, G.L. (1977). A simplification of the protein assay method of Lowry et.al. which is more generally applicable. Anal. Biochem. 83, 346-356.\n5. Schacterle, G.R. and Pollack, R.L. (1973). A simplified method for the quantitative assay of small amounts of protein in biologic material. Anal. Biochem.\n51, 654-655.\n6. Hartree, E.E. (1972). Determination of protein; A modification of the Lowry method that gives a linear photometric response. Anal. Biochem. 48, 422-427.\n17. Creighton, T.E. (1984). Chemical nature of polypeptides, in Proteins. New York: W.H. Freeman and Co., pp 1-60.\n18. Sengupta, S. and Chattopadhyay, M.K. (1993). Lowry’s method of protein estimation: some insights. J. Pharm. Pharmacol. 45, 80.\n19. Lo, C. and Stelson, H. (1972). Interference by polysucrose in protein determination by the Lowry method. Anal. Biochem. 45, 331-336.\n20. Neurath, A.R. (1966). Interference of sodium ethylenediaminetetraacetate in the determination of proteins and its elimination. Experientia 22, 290.\n21. Kuno, H. and Kihara, H.K. (1967). Simple microassay of protein with membrane filter. Nature 215, 974-975.\n22. Morrissey, T.B. and Woltering, E.A. (1989). Sodium oxalate corrects calcium interference in Lowry protein assay. J. Surg. Res. 47(3), 273-275.\n23. Sargent, M.G. (1987). Fiftyfold amplification of the Lowry protein assay. Anal. Biochem. 163(2), 476-481.\n26. Dawson, J.M. and Heatlie, P.L. (1984). Lowry method of protein quantification: evidence for photosensitivity. Anal. Biochem. 140(2), 391-393.\n27. Fryer, H.J.L., Davis, G.E., Manthorpe, M. and Varon, S. (1986). Lowry protein assay using an automatic microtiter plate spectrophotometer. Anal.\nBiochem. 153(2), 262-266.\nshould be taken to subject the samples to the same\nlevel of illumination during the procedure.26\nSeveral modifications of the original Lowry procedure\nhave been reported. For example, modifications\nhave been made to simplify the procedure4,5\nand to improve the following: linearity of response;\n6 reproducibility and sensitivity;23 stability\nand chemistry of color development; stability of\nthe biuret reagent;2,5 and speed.27 Other modifications\nhave dealt with interfering substances7 and\napproaches to the analysis of protein samples in\nthe presence of biomaterials such as lipids.\nMuch has been published regarding substances\nthat interfere with protein determination using the\nLowry procedure. Compounds commonly known\nto interfere with the Lowry assay include: detergents\nand carbohydrates;8,19 glycerol, Tricine and\nEDTA;20 Tris;21 potassium and sulfhydryl and disulfide\ncontaining compounds;9 magnesium;21 and\ncalcium.22\nThe addition of oxalate to