How to Use the Z.TEST Function in Excel

How to Use the Z.TEST Function in Excel Hypothesis tests are one of the major topics in the area of inferential statistics. There are multiple steps to conduct a hypothesis test and many of these require statistical calculations. Statistical software, such as Excel, can be used to perform hypothesis tests. We will see how the Excel function Z.TEST tests hypotheses about an unknown population mean. Conditions and Assumptions We begin by stating the assumptions and conditions for this type of hypothesis test. For inference about the mean we must have the following simple conditions: The sample is a simple random sample.The sample is small in size relative to the population. Typically this means that the population size is more than 20 times the size of the sample.The variable being studied is normally distributed.The population standard deviation is known.The population mean is unknown. All of these conditions are unlikely to be met in practice. However, these simple conditions and the corresponding hypothesis test are sometimes encountered early in a statistics class. After learning the process of a hypothesis test, these conditions are relaxed in order to work in a more realistic setting. Structure of the Hypothesis Test The particular hypothesis test we consider has the following form: State the null and alternative hypotheses.Calculate the test statistic, which is a z-score.Calculate the p-value by using the normal distribution. In this case the p-value is the probability of obtaining at least as extreme as the observed test statistic, assuming the null hypothesis is true.Compare the p-value with the level of significance to determine whether to reject or fail to reject the null hypothesis. We see that steps two and three are computationally intensive compared two steps one and four. The Z.TEST function will perform these calculations for us. Z.TEST Function The Z.TEST function does all of the calculations from steps two and three above. It does a majority of the number crunching for our test and returns a p-value. There are three arguments to enter into the function, each of which is separated by a comma. The following explains the three types of arguments for this function. The first argument for this function is an array of sample data. We must enter a range of cells that corresponds to the location of the sample data in our spreadsheet.The second argument is the value of  ÃŽ ¼ that we are testing in our hypotheses. So if our null hypothesis is H0:  ÃŽ ¼ 5, then we would enter a 5 for the second argument.The third argument is the value of the known population standard deviation. Excel treats this as an optional argument Notes and Warnings There are a few things that should be noted about this function: The p-value that is output from the function is one-sided. If we are conducting a two-sided test, then this value must be doubled.The one-sided p-value output from the function assumes that the sample mean is greater than the value of  ÃŽ ¼ we are testing against. If the sample mean is less than the value of the second argument, then we must subtract the output of the function from 1 to get the true p-value of our test.The final argument for the population standard deviation is optional. If this is not entered, then this value is automatically replaced in Excel’s calculations by the sample standard deviation. When this is done, theoretically a t-test should be used instead. Example We suppose that the following data are from a simple random sample of a normally distributed population of unknown mean and standard deviation of 3: 1, 2, 3, 3, 4, 4, 8, 10, 12 With a 10% level of significance we wish to test the hypothesis that the sample data are from a population with mean greater than 5. More formally, we have the following hypotheses: H0: ÃŽ ¼ 5Ha:  ÃŽ ¼ 5 We use Z.TEST in Excel to find the p-value for this hypothesis test. Enter the data into a column in Excel. Suppose this is from cell A1 to A9Into another cell enter Z.TEST(A1:A9,5,3)The result is 0.41207.Since our p-value exceeds 10%, we fail to reject the null hypothesis. The Z.TEST function can be used for lower tailed tests and two tailed tests as well. However the result is not as automatic as it was in this case. Please see here for other examples of using this function.

How to Get a Birthday Cake Delivered to a College Dorm

How to Get a Birthday Cake Delivered to a College Dorm Whether youre a parent or a friend, sending a birthday cake to a students dorm room can be one of the most thoughtful things you can do during those stressful college years. Parents worry about their kids while theyre away, and friends want to celebrate in style with fun surprises. Whether youre long distance or just want to make your kid or friend smile, sending a little celebratory gift can make all the difference. Delivering Birthday Cakes to Dorms The first thing you want to do is see if the college you want to send a cake to offers special orders for birthday treats through their dining halls or student life services. This would be a fast solution, so scouting out the possibilities is key. Simply inquire when you visit the campus during orientation or give them a quick call. At the University of Delaware, for instance, you can send a YoUDee Gram –a 10 to 15-minute visit by the school mascot, who is a giant blue chicken that arrives at the students dorm with balloons, an autographed photo, and more than a little comic pizazz. Parents and friends can also call the University of Delawares dining hall to order a personalized birthday cake for dorm delivery or pick up. In fact, other colleges like Stanfords parent association  deliver birthday cakes, balloons, and flowers, as a fundraiser for the college endowment fund. Bakery Deliveries Some college town bakeries deliver on campus. However, if you cant find a local patisserie, there are plenty of bakers who will ship their wares overnight or via two-day mail. Simply check in with the campus mail room to see if any restrictions apply. Some accept FedEx or UPS overnight, while others prefer US postal service deliveries. Get creative with all the fun possibilities for your cake send by drawing inspiration from other colleges: Arizona’s Fairytale Brownies  mails a birthday box with brownies, a teddy bear, a kazoo, and a pin-the-tail-on-the-donkey game for around $50.The Delaware-based SAS Cupcakes ships assorted vanilla, triple chocolate, and red velvet cupcakes decorated for birthdays or Greek life events, accompanied by little flags with your child or friends Greek letters. Delivered by the dozen, this delivery costs around $45. A Homemade Birthday Box Forget all the headaches and assemble your own birthday-in-a-box. Frosted cakes dont do well in the mail, so you can bake a cake. The moister the cake, the better. Consider flavors like  pumpkin, carrot, or banana. Once youve baked your cake, youll want to make sure its wrapped before you ship it off. Include little additions to your care package, like a simple can of supermarket frosting, a box of candles, and a birthday tiara. Alternatively, you can bake up a batch of chocolate cookies that are  decorated to look like cupcakes, and ship them off. For something extra, add a birthday card or a small gift.

Personal Journey Essay Example | Topics and Well Written Essays - 1250 words

Personal Journey - Essay Example The time we are kids, we have our own choices and preferences about anything we come across without containment parts imposed by elders in the family or the peer group we live in. As Erikson says, at each stage, there must develop an ego capability for the further development of personality (Slee 2002, p.53). I remember the days which I was always free from entrustments of heavy burdens or ethical values to be added to my life unlike now. I had my schooling done in a comparatively small town with not many things to speak great bout those days. I can never say that I was at compromise with anything I longed for. I used to have good and fashionable clothes and lots of fun with very good friends. I must say, they should be the real gift of God. We had resourceful teachers to guide us through the high school education where the school was rated one of the top ten schools in the state. Since my physique was quite athletic, I was directed to join various training campaigns to get trained for competitive events at different levels. At times I was successful, but never did I have the feel that I would ever become a sports man. It may be the case because; I was much concerned about the humane elements of life. As an innate nature, I always liked to be of some help to people around me. Even today, I feel puzzled when I try to consolidate my present life with what I expected myself to be. It is for sure, my being a doctor was not an overnight affair. It took me several years of study and researches to become at lest what I am now. A clear – cut study of evolutions happened in me may get you the idea about how people change themselves through different ages. I would never like to accept that I have done something to change myself; therefore, I can say that life changes on its way with condition pertaining to stages of life. According to Erikson, â€Å"the adulthood stage focuses

Variations on the Modern Essay Example | Topics and Well Written Essays - 3000 words - 1

Variations on the Modern - Essay Example The aim of this study is to discuss different versions of modern architecture movements in Italy and Scandinavia in order to show how modern architecture responded to the political and cultural subtexts. Modern architecture was flourished later in both Italy and Scandinavia than Germany, Holland, France and Russia. William J. Curtis notes that Modernism's influence was slight in Scandinavia in the 1920s1 and it formed relatively late in Italy2. Furthermore, both Scandinavia and Italy brought their own interpretation to the â€Å"international style†. However, their similarities end here; since their political, cultural and also ecological conditions were extremely different. While modern architecture emerged in Fascist Italy ruled by a dictator, democratic welfare states prevailed in Scandinavia at that time; hence, there was a stark difference between the political climates of Italy and Scandinavia. Their cultures also differed; whereas nationalistic tendencies and nostalgia for the Roman heritage were predominant in Italy, communal values were strong in Scandinavia. In line with their differences, they both developed a different variation of Modernism. While Italian Modernism highlighted nationalism and magnanimous Roman heritage; Scandinavia adopted a modernism with a human face stressing organic and natural life. As a matter of fact, in Italy, modernism grew in two directions: Noveconto and Italian Rationalism. The Classical Novecento movement, represented by Giovanni Muzio, paved the way for the development of Italian Rationalism represented by â€Å"gruppo 7†3. Sebastian Larco, Guido, Frette, Carlo Enrico Raba, Adalberto, Luigi Figini, Gino Pollini and Guiseppe Terragni formed Gruppo 7 in 19264. Throughout the 1930's, both Novecento and Italian Rationalism coexisted as alternative variations of modernism. Although Novecento, originated in Milan, used modern technology of concrete construction, it was highly committed to the traditional Itali an house. Gio Ponti, the famous architect and editor of the magazine of the Italian house Domus, described Italian house as setting for Italian life as follows: â€Å"the place that we have chosen for enjoying our life†5. Ponti's description highlights the stark difference between Novecento and Le Corbusier's â€Å"international style†, since Le Corbusier defined the house as â€Å"a machine for living in†. While Ponti's approach stressed the organic and humanist aspect of the house, Le Corbusier's definition was more mechanistic. Furthermore the Novecento houses were more decorative and furnished in Italian taste, while â€Å"the international style† was against any ornaments. Indeed, modern Milan houses incorporated common features of traditional Italian chimneys and sundials6. Although Italian Rationalism could be regarded as more radical than Novecento and closer to the spirit of machine civilization, it was still â€Å"fully contextual as well, rela ting to historical Italian culture†7. Besides Italian culture, Italian Rationalism was also intertwined with Fascist nationalism. It was not just Italian Rationalists were ardent fascists, but their work also reflected the Fascist ideology; although The Italian Fascist Party's relation to Italian Rationalism was ambivalent. Giuseppe Terragni's Casa del Fascio could

Purification of Immunoglobulin G by Ion-Exchange

Purification of Immunoglobulin G by Ion-Exchange Purification of Immunoglobulin G by Ion-Exchange Chromatography and Immunoelectropheresis William McTavish Joseph Zappa Introduction Immunoglobins or, Antibodies, are soluble proteins secreted from host differentiated plasma cells that target and eliminate specific antigens to protect the host from disease (Jakoby, 1971). There are five isotypes of immunoglobulin: IgM, IgD, IgA , IgE and IgG, with IgG being the most prominent antibody found in blood circulation of the host. The purification of specific antibodies has led to the development of techniques such as western blotting; where desired proteins can be targeted by monoclonal antibodies engineered for a specific affinity for that protein( Burnette, 1981). The basis of immunoglobulin purification can begin with a technique of â€Å"salting out†, used vastly for precipitating organic molecules and is the first step in protein purification (Tsutomu and Timasheff, 1984). Immunoglobins are small soluble proteins that can be found within serum that is removed from a blood sample taken from the host. Hydrophillic immunoglobins contain amino acids that are polar or possess an ionic charge. Counter ions in the serum of the host are attracted to these polar and ionic charges making the proteins soluble in the solvent. By destabilizing the intermolecular forces between the immunoglobins and the serum solvent there can be an induced precipitation of these proteins. Ammonium sulfate is a highly used compound in salting out procedures, for when ammonium sulfate dissociates, the large sulfate ions form hydrogen bonds between the polar molecules found in the serum (Tsutomu and Timasheff, 1984). The quenching effect of sulfate removes hydrogen bonds and intermolecular forces away from the protein molecules, forcing them to form bonds between one another. This forced intermolecular bonding between proteins causes an accumulation of aggregated proteins and eventually, at the right concentration of salt, precipitation out of solution (Tsutomu and Timasheff, 1984). Although the precipitation of immunoglobulin from host serum with Ammonium sulfate is an efficient procedure for isolating globin, it does not allow for the accurate determination of a specific isotype of immunoglobulin. Ion exchange chromatography is a prominent technique used to acquire a single desired protein, including a specific isotype of immunoglobins. All molecules, including immunoglobulin that have ionizable groups have a net surface charge that is highly dependent on the environmental pH in which that molecule is in. The pH of an environment can dictate the amount of charge present on a molecule, whether it is more positive or more negative, as well as neutral (Grodzki, and Berenstein, 2010). The neutral point, where all positive charges cancel out the negatives is expressed as the pI of the molecule (Grodzki, and Berenstein, 2010). Since all proteins vary in their pI they will express specific charges at any specific pH. This characteristic of immunoglobulin is utilized in Ion exchange chromatography to isolate specific isotypes even if they vary only slightly in charge. IgG, as well as other isotypes of Ig, have a pI occurring near neutral pH so Anion exchange resins are often used for this type of chromatography. Anion Exchangers utilize resin that contains positively charged functional groups that act as counter ions towards protein being eluted through the column (Determann et al. 1969). With the resin set at a specific pH, the proteins that are most positive will exit the column first due to the repulsion of charges between the positive protein and positive resin. The next proteins to elute will be the neutral ones followed by the negatively charged proteins. Proteins are removed in this manner by constantly adding more of the buffer the column is immersed in. By adding more buffer there is an increased competition for associating with the resins charges, which in turn dissociates protein from the resin and further elutes them through the column (Determann et al. 1969). Not only does the charge of the beads matter but also the flow and porosity of the resin, alternations of these can allow for either a more broaden column exchange or a far more refined one. Diethyl aminoethyl (DEAE)-cellul ose is a commonly used resin for anion exchanging due to its higher porosity and positive functional groups that allows for better flow properties of the column. Increased flow rate allows for separation of more bulky and crude proteins, such as crude immunoglobulin, and aids in a higher resolution of separated proteins (Determann et al. 1969). Once several fractions of the column elution is collected there is many ways to identify which fraction is most likely containing the desired protein of isolation including determining the optical density of the fractions with a spectrophotometer. The OD of Immunoglobulin and other proteins can be determined by selecting a specific wavelength of light and beaming it through the elution fraction and recording the amount of transmitted light via photoreceptors (Edelhoch, 1967). A common wavelength used for identifying immunoglobulin is 280nm, this wavelength is absorbed by the amino acid tryptophan in proteins. Absorption of this wavelength in protiens makes it a proportional reduction of transmitted light based on the concentration of protein present in the column fraction (Edelhoch, 1967). The higher the reduction in transmitted light, the higher the OD reading for a fraction. A fraction of elute from Ion exchange chromatography may contain the desired Immunoglobulin G, but to further prove this, a technique called Immunoelectrophoresis (IEP) can be used to confirm the purity of Immunoglobulin fraction. Immunoelectrophoresis is a two-part technique that combines the use of electrophoresis and zone of equivalence of immune complexes to determine a positive result. Electrophoresis is another basic technique used in separating proteins based on size and charge to obtain separate sections of protein in agar gel or other resins such as polyacrylamide in SDS-PAGE techniques.(1) Proteins separate into a gradient of smallest more positive charged towards the cathode to smallest most negative charged towards the anode, with the larger, less charged proteins in the middle gradient. (Serwer and Wright, 2012). After protein separation has occurred in the welled samples, there is addition of antibody specific for certain protein that may be isolated out of the samples used in the experiment. If proteins are present that are the target of affinity for the added antibodies there will be association of antibody:antigen complexes. These complexes will form in the agar gel and at the proper gradient of both antibody and antigen concentrations there will be precipitation of these complexes out of the solution (Slater, 1975). This correct gradient is called the zone of equivalence and is frequently used in determining the presence of desired protein molecules, including immunoglobulin (Slater, 1975). Several other techniques are used in isolating proteins, an extremely prominent technique is the use of Antibodies themselves in Immunofluorescence (IF). Antibodies are engineered to contain a specific affinity towards a desired molecule, protein or even a whole cell. IF can work in either two ways: the first involves a single antibody engineered towards a desired antigen containing a flurochrome itself and emits fluorescent light to be detected. The second contains a secondary antibody that has affinity for the primary antibody binding to an antigen, this secondary antibody is the one that contains the fluochrome for detection (Johnson, 2006). In either of these techniques there is the advantage of staining samples of proteins or cells and identifying not just a single antigen but several with several different antibodies. This technique is extremely useful for identifying proteins in cell structures as well as identifying the presence of proteins in biological systems. Methods and Materials All methods used in this experiment can be located in the Immunology Laboratory Manual cited in references. There were two major alternations to the Immunoelectrophoresis experiment; There was a time of 1.5 to 2 hours allowed for electrophoresis of the agar slides instead of 1 to 1.5 hours. There was also an expansion of time from 24 hours to 48 hours allowed for the IEP slide to rest in a cold room before soaking in 1% NaCl solution. Results A high concentration of IgG was isolated in the third elution fraction from DEAE-cellulose Ion exchange chromatography. Optical density of six Ion exchange chromatography elution fractions were taken with a spectrophotometer to determine protein concentration at a wavelength of 280nm (Fig 1). The highest optical density was observed in the third elution fraction (Fig 1). This illustrates that the largest concentration of protein at a similar charge was eluted at the third fraction of the Ion exchange experiment. Figure 1. Third fraction of DEAE-celluose elution scored the highest optical density. All fractions were tested with spectrophotometry and optical density measurements were taken at a wavelength of 280nm (Fig 1). Results are shown as single values of optical density (OD) and relate to the amount of protein concentration in each fraction. (Fig 1) Immunoelectrophoresis of isolated protein reveals presence of purified IgG in response to Goat anti-rabbit serum Presence of Rabbit Immunoglobin was tested for using Immunoelectrophoresis with Goat anti-rabbit serum. Normal rabbit serum and purified fraction of protein were welled on a 1% agar slide and proteins were separated based on charge via electrophoresis. Anti-rabbit serum was added and results were taken for precipitation of immune complexes 48 hours later (Fig 2). Thin white lines between the wells and trough are precipitated immune complexes and thus show a positive test for rabbit immunglobins (Fig 2). Figure 2. Precipitated immune complexes reveal immunoglobin presence in normal rabbit serum and purified fraction. Proteins were isolated based on charge via electrophoresis to isolate specific proteins. Goat Anti-rabbit serum was added as antibody for rabbit immunoglobin and incubated for 48 hours. Distinction of grey and white bands are positive results regardless Discussion Purified Rabbit Immunoglobin G was isolated from Normal rabbit serum using DEAE-cellulose ion exchange chromatography and Immunelectropheresis with Goat anti-rabbit serum. Once the majority of proteins were salted out of the normal rabbit serum, Ion exchange chromatography was used to separate all proteins from the sample of crude globin. Since immunoglobin proteins are soluble in the blood and are near neutrally charged at philological pH, a large amount of protein was expected to elute roughly half way through the Ion exchange chromatography regardless of using anion or cation exchange columns (Grodzki and Berenstein, 2010). These results occurred for the DEAE-cellulose Ion exchange column used to separate crude rabbit globulin in our experiment. The third elution fraction, of six, contained the highest optical density when evaluated with the spectrophotometer at 280nm. Optical density is related to the concentration of protein in a sample, thus the fraction containing the highest amount of protein was the third fraction which was collected half way through the elution process. Although the method of determining sample concentrations for proteins can vary, these results can be seen in similar protein isolation studies such as Ye et al. article Isolation of lactoperoxidase, lactoferrin, ÃŽ ±-lactalbumin, ÃŽ ²-lactoglobulin B and ÃŽ ²-lactoglobulin A from bovine rennet whey using ion exchange chromatography. The protein isolated is presumed to be the globulin isotype Iummogloublin G, this is due to the nature of circulating antibodies found in the serum of the rabbit. The most prominent antibody isotype circulating in the blood is IgG, which binds to antigens, forming immune complexes as well as aiding in many other immune system mechanisms such as compliment activation, opsonization and etc (Collins and Jackson, 2013). Immunoelectrophoersis with Goat anti-rabbit serum was used next to determine whether or not the isolated protein in the third elution fraction is Immunoglobulin G. The nature of this experiment depends on two key process gel electrophoresis and precipitation of Immune complexes. If electrophoresis is preformed properly there should be a separation of proteins based on charge/size from the samples that were welled on the agar covered slide used in the experiment; creating small zones of protein purity along the slide (Slater, 1975). Since the eluted fraction sample should only contain one kind of protein and is roughly pure, there should only be one zone of protein sample, where the normal rabbit serum, containing an array of different proteins, will electrophoresis out into several different zones of protein. Determining these zones of protein was done by adding Goat anti-rabbit serum and allowing diffusion into the gel to create zones of equivalence between antibody and antigen, thu s precipitating the complex to be seen visibly (Serwer and Wright, 2012). For a positive result on the purity of the fraction sample only a single precipitation line formed at the zone of equivalence would be seen. The results for the purity of the fraction sample was conclusive with the above expectations, only a single faint precipitated line was seen on the gel; therefore re-enforcing that there is only a single protein isolated from the Ion exchange elution phase. The single protein isolated is promptly IgG due to it’s response to the anti-Rabbit serum containing anti-rabbit globulin. Immunelectrophoresis was used in this experiment to confirm the presence of IgG in the eluted fraction sample taken from DEAE-cellulose ion exchange chromatography. The reason this method was used was due it’s simplicity in determining specific immune complexes and thus re-ensuring purity. It is relatively quick in determining the presence of antigen, in this case the immunoglobin G of rabbit, and gives results ready to be read visually, lacking the need for software or other means of identification. The draw back of this technique is that it takes some practical skill in preparation and is only useful in identifying the purity of one sample at a time. Techniques such as western blotting would be more efficient for studies that desire more than a single purity such as Yang et al’s article Correlation between the overexpression of epidermal growth factor receptor and mesenchymal markers in endometrial carcinoma. An alternation to this experiment could be made in the chroma Purification of Immunoglobins is an extremely useful procedure. Being able to isolate specific classes of Immunoglobulin aids in research of host immune deficiencies such as the research done by Tamura et al in their article Tumor-Produced Secreted Form of Binding of Immunoglobulin Protein Elicits Antigen-Specific Tumor Immunity as well as many other fields of host immunity and clinical research. Successful purification and crystallization of Immunoglobulin has also allowed for insight on how host immune systems respond to infection and the biological processes that take place in these responses. References Jakoby, W.B. 1971. Cystallization as a purification technique, Enzyme Purification and Related Techniques, Methods in Enzymology. 22: 246-252 Determann, H. Meyer, N. Wieland, T. 1969. Ion exchanger from pearl-shaped cellulose gel. Nature 223: 499-500 Edelhoch, H. 1967. Spectrospoic determination of tryptophan and tyrosine in proteins Burnette, N.W. 1981. â€Å"Western Blotting†: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Analytical Biochem 112: 1935-203 Tsutomu A. and Timasheff, S.N. 1984. Mechanism of protein salting in and salting out by divalent cation salts: balance between hydration and salt binding Biochemistry(23)25:5912-5926 321 -Grodzki, A.C. Berenstein, E. (2010) Antibody Purification: Ion-Exchange Chromatography Methods in Molecular Biology 588: 27-32 Slater, L. 1975. IgG, IgA and IgM by formylated rocket immunoelectrophoresis. Ann Clin Biochem 12 (1) : 19-22, 24 Yang, W.N.Ai, Z.H. Wang, Xu, J.Y.L. Teng, Y.C. 2014.Correlation between the overexpression of epidermal growth factor receptor and mesenchymal makers in endometrial carcinoma. J Gynecol Oncol. 25:36-42. 47 Collins, A.M. Jackson, K.J.L. 2013. A temporal model of human IgE and IgG antibody function. Front Immunol 4: 225 Ye, X. Yoshida, S. Ng, T.B. 2000. Isolation of lactoperoxidase, lactoferrin, ÃŽ ±-lactalbumin, ÃŽ ²-lactoglobulin B and ÃŽ ²-lactoglobulin A from bovine rennet whey using ion exchange chromatography The international journal of Biochemistry Cell biology 32 (11-12): 1143-1150 22 Nydegger, U.E. Lambert, P.H. Gerber, H. Miescher, P.A. 1974. Circulating Immune Complexes in the Serum in Systemic Lupus Erythematosus and in Carriers of Hepatitis B Antigen QUANTITATION BY BINDING TO RADIOLABELED Clq Circulating immune complexes in the serum in Systemic Lupus Erythematosus and in carriers of Hepatitis Antigen B Quantitation by binding to Radiolabelled Clq. J Clin Invest.  54(2): 297–309. Serwer, P. Wright, E.T. 2012. Agarose Gel Electrophoresis Reveals Structural Fluidity of Phage T3 DNA Packaging Intermediate. Electrophoresis 33 (2): 352-365 101-Johnson, I.D. 2006. Practical considerations in the selection and application of fluorescent probes. In: Handbook of biological confocal microscopy, 3rd ed. (J.B. Pawley.ed), Plenum Press. new York. p.362-3. Circulating Immune Complexes in the Serum in Systemic Lupus Erythematosus and in Carriers of Hepatitis B Antigen QUANTITATION BY BINDING TO RADIOLABELED Clq

Formative Writing †Slumdog Millionaire Essay

The film ‘Slumdog Millionaire’ by British born director Danny Boyle, gives a particular insight into life in India, and more specifically the city of Mumbai through the use of setting. It is this cultural backdrop presented through the perspective of foreigner that not only makes the film special, but also sparked a lot of debate whether the image revealed is an accurate portrayal of India. The film attempts to show the shocking and disturbing realities that occur in India, including poverty, injustice, slums, gang culture and prostitution. An example of one of these realities being depicted is in the scene where Jamal and Salim have been captured by the gangster Maman who plans to blind Jamal in order to make him a profitable beggar as he will evoke more sympathy if blind. The setting of the scene is outside a remote building where the gangsters keep the children at night. These children are placed away from the rest of civilisation showing how they are unwanted and are outsiders. The lighting is minimal making it dark, eerie and scary which is also coupled with fast pace camera shots which are predominantly close-ups on things such as the acid, Maman’s face and one of his accomplices cracking his knuckles. All of these features work together in order to create an intimidating impression on the viewer as we don’t get the full perspective echoing how the children are being tricked and deceived. Salim watches one of the boys eyes being burned yet the viewer doesn’t get to see this, instead the horror is echoed through Salim’s physical reaction as he vomits. It appears that the director wants to shock the audience and present the horrors present in Indian culture, yet he doesn’t show it physically being done, creating a barrier which shields the western audience at all times. Maman asks Salim whether he wants ‘the life of a Slumdog or a man?’ This gives the impression that all Indian men should want to be and are like Maman who is evil and corrupt, giving a negative representation of men in India.

William Shakespeare s Romeo And Juliet - 1150 Words

Romeo+Juliet, a kaleidoscopic film directed by Baz Lurmann, is an intriguing modern interpretation on Shakespeare’s 16th century romantic tragedy, Romeo and Juliet, which has been appropriated to suit the audience and context of modern day society. Lurmann said in an interview, â€Å"Shakespeare had an amazing genius for capturing who we are and revealing it to us. My job is just to re-reveal it.† Lurmann successfully appropriated Shakespeare’s original ideas of conflict, violence, love and death, which remain woven through the storyline with the use of characters, setting, theme and dialogue, Romeo and Juliet has been transformed into a modern-day classic, in the form of Baz Lurmann’s Romeo+Juliet. Baz Lurmann chose a modern day city as the†¦show more content†¦In the film, the â€Å"hot, sexy, violent, Catholic city† Verona was re-contextualised to suit modern society, resulting in the name â€Å"Verona Beach.† In both the play and the film – setting is a convention that influences the audience’s views of the plot. The film’s beginning instantly provides the audience with visual idea of the city, with it’s montage packed with snippets of police chases and helicopter pursuits, Religious icons like the Christos Statue, panning of a bustling city, various zooming shots of The Montague and Capulet building signs and the flashes of bold Newspaper headlines. This montage partnered with the music, creates the perfect mood to set the scene of Romeo + Juliet. The viewers are presented with a relevant society that is chaotic, spicy and religious, yet it remains true to its initial setting, â€Å"fair Verona.† The language Shakespeare uses when Romeo is first introduced to the audience in Verona is quite childlike and immature. Romeo illustrates to the audience his current state of mind with a progression of contradictory statements, intertwining both the wonders of love and the stresses of unrequited love. â€Å"O brawling love, O loving hate.† The fact that Romeo chooses to express such immense emotions for Rosaline, a lady whom he barely knows, shows the audience not only his immaturity but also his craving for a deeper love. Shakespeare’s use of traditional poetry in the beginning of