Photographic Connections

Creative Commons licensed image posted at Flickr by Leo Reynolds

Creative Commons licensed image posted at Flickr by Leo Reynolds

Activity

  1. Take a picture of something in your room. It can be anything–your favorite t-shirt, a poster, your laptop, a picture of another picture (whoooooa–Inception, man….), anything. Go wild.
  2. Upload that photo to your computer and place it in a document.
  3. Look at the writing assignment prompt your professor gave you. Write the main concept of the prompt beneath the photo you uploaded.
  4. Do a search online that combines the content of your photo with the main concept of the assignment prompt. For example, if you took a picture of your shoes and the main concept of your assignment prompt requires that you talk about social economics, you might search for “social economic status and shoes,” “shoes and social economics,” and “footwear and class stratification.” Notice with the last example we used synonyms for our words to possibly uncover some new insights.
  5. Find an article or website in your search that demonstrates a connection between your photo and your assignment prompt. This is a starting point for your research.
  6. Share-out: Post your image, main assignment prompt concept, and the best website URL you found in the comments thread. Format it as follows: [image] + [main assignment concept] = website URL.

22 thoughts on “Photographic Connections

  1. Chem442s15a Chem442s15a

    Plants + IImmunoglobulins = http://www.sciencedirect.com.proxy.lib.odu.edu/science/article/pii/S0734975011001303
    Recombinant proteins have been very useful in the medical field, genetics, and biotechnology. Most of these are synthetically made from human hormones, or they can also be made from animal extract. However, in the last 20 years plant-based systems have been used as the main source of recombinant protein because they have many industrial applications such as vaccine production, enzyme synthesis, and developing new medications. The purification and the making of protein recombinant success depends on the type of plant host system. There is a seed-crop system and leaf based system. The seed-based system provides recombinant proteins that are expressed in cytokines, cell culture proteins, vaccines, and industrial enzymes. The method used to purify the seed-based system is by using fractions. This method uses dry milling, dry fractionation, and wet milling. Out of the three different methods, wet milling provides the highest protein purity since it can separate the protein better. Although, seed crops have many advantages over microbial fermentations and mammalian cell cultures they have a low biomass yield per unit surface when compared to the leaf-based system. There is also a fear of cross contamination, mixing between transgenic and non-transgenic grains. When purifying plants from the leaf-based system they give a high biomass yield. Tobacco, for instance, is the most leaf-bases system used for the production of recombinant proteins. Although this system provides a high biomass, the disadvantages of using leaf extracts is that they have proteolytic activities, phenolic compounds, and chlorophyll derived pigments. These can interfere in the purification process by affecting the quality and yield of the purified protein since a multistep purification process has to be accomplished.

    Attachment:

  2. Chem442s15f

    Research and study of microbial pathogenesis reveal the profound beauty of immunity in humans. Surface proteins on some bacteria will bind to specific regions on immunoglobulin. Using methods of protein purification, the complex can be isolated and introduced into animals to further study its virulence. These studies are an attempt to develop new antimicrobial medications that will be effective against antibiotic resistant bacterial infections.

    [Microbiology textbook] + [Protein Purification and Microbiology textbook] = [http://www.ncbi.nlm.nih.gov/books/NBK8448/]

    Attachment:

  3. Nikisha Hartin

    My Dog+Immunoglobulins=http://www.sciencedirect.com/science/article/pii/S0165242798001329#
    This article discusses the concentration of antibodies in the salvia, tears and bile of different types of canines. Serums were tested and examined on how much immunoglobulins were present for instance, IgG, IgA etc.

    Attachment:

  4. William Wall

    Stress + Immunglobulins = http://www.sciencedirect.com/science/article/pii/S0306453097000425

    Every university student has gone through the troubles of stress and felt its impact. Whether it’s studying for a big exam, or desperately trying to get a lab report turned in on time, stress is a big part of college. But all that stress can wear on the body, and put it in a constant state of alert. In response, the body releases immunoglobulins of all kinds to combat the stress. One immunoglobulin in particular, the dimeric immunoglobulin A, can inhibit the actions of other immunoglobulins, and thus reduce body immune response. This can provide credence to the adage that too much stress can make you more susceptible to illness.

    Attachment:

  5. chem442s15d

    Horses+ Immunoglobulins= http://www.jasbsci.com/content/3/1/18

    Immunoglobulins are essential for the animal immune response and are expressed in mammals, amphibians, reptile, birds, etc. Immunoglobulins are usually expressed in B cell receptors or secreted from an antibody. The immunoglobulin structure consists of two identical light chains and two heavy chains. This article discusses the diversity of immunoglobulins (Ig) and isotopes that are expressed in livestock such as horses. Horses are a predominant mammalian species that express a full-range of Ig heavy chains. The genomic sequence of a horse shares a degree of homology with human than artiodactyl genes. Analysis of horse genes indicated that they have evolved by gene duplication and unequal crossing. Through this research, scientists have determined that between a comparison with humans and domestic animals, the animals have a smaller germline V gene repertoire. In the future they hope to understand the genetic components of animal immune system in order to study disease control in farm animals.

    Attachment:

  6. Chem442s15n

    Magnets + Protein Purification = http://www.ncbi.nlm.nih.gov/pmc/articles/PMC544596/

    Magnetic separation is a relatively simple technique to perform. All purification steps occur in 1 container, which reduces the likelihood of spillage or contaminants. A magnetic carrier with affinity to the target molecule is introduced into the solution. This solution does not need to be refined prior to using this technique. During the incubation period the magnetic carrier binds to the target molecule. The sample is then washed and removed with a magnetic separator. Protein A Mag Sepharose are beads with magnetic properties that are used in immunoprecipitation or pull-down purposes. Sepharose is agarose in bead form. In immunoprecipitation the magnetic bead is attached to either A/G protein or a NHS activated bead. This complex then binds to antibodies. These antibodies then bind to the target protein. The complex is then washed and the target is eluted.

    Attachment:

  7. Chem442s15l

    Cat + Immunoglobulin = http://www.ncbi.nlm.nih.gov/pubmed/12126130

    A case study of a 5-mo old female cat being successfully treated for severe skin ulcers by human IV immunoglobulin after the cat’s condition continued deterioriating despite routine administration (rabies vaccine, anthelmintic, and ear medication). It is interesting to investigate how treatments can be used among species to treat different diseases. Another aspect of this may be using chemicals and biomolecules from other species to engineer treatments for human disease, as is the case in anti-venom.

    Attachment:

  8. Chem442s15s

    Exercise and Immunoglobulins

    Previous to this assignment, I believed that exercise could only help your immune system. This is the attitude held by many athletes. An article on the effects of exercise on immunoglobulins discussed this topic in detail. Researchers found that acute moderate exercise increased serum immunoglobulin levels. It was also found that the serum IgM levels were the most effected by acute submaximal exercise. Between athletes and non-athletes, resting serum immunoglobulin levels are similar; however, elite athletes have been seen to have lower levels in both serum and secretory immunoglobulins. For example, it was found that IgA concentration in nasal and salivary secretions was decreased by nearly 70% for at least 18 hours after heavy exercise. This in turn leads to an increased risk of infection for elite athletes. The data presented suggested that our immune system is temporarily weakened after prolonged endurance exercise. Repeatedly exerting near maximal levels of energy while being exposed to pathogens along with other stressors increase the risk of infection. This is important for athletes and coaches to be aware of to stay healthy and reduce risk of infection, which is very common among teams.
    There are five classes of immunoglobulins, or antibodies: IgA, IgD, IgE, IgG, and IgM. IgA is found mostly in secretions and serves as part of the body’s first line of defense against pathogens entering mucosal surfaces. IgD is found in serum but its function is still unknown. IgE is also found in serum and is related to immune response against allergens. IgG has the highest concentration in the body and is found in serum. It is also the only immunoglobulin that can pass through the placenta and is involved in the body’s secondary immune response. IgM is found in serum and is produced in the primary immune response. IgM and IgG are the body’s major defenses against most infectious diseases.

    References
    http://ovidsp.tx.ovid.com.proxy.lib.odu.edu/sp-3.14.0b/ovidweb.cgi?T=JS&PAGE=fulltext&D=ovft&AN=00007256-199111030-00003&NEWS=N&CSC=Y&CHANNEL=PubMed
    http://eds.b.ebscohost.com.proxy.lib.odu.edu/ehost/pdfviewer/pdfviewer?sid=d259d14d-f21b-4dc4-9a74-5c3696d93bb1%40sessionmgr115&vid=1&hid=126

    Attachment:

  9. Nikisha Hartin

    My Dog+Immunoglobulins=http://www.sciencedirect.com/science/article/pii/S0165242798001329#

    Attachment:

  10. Chem442s15r

    Seashells & Immunoglobins: insights into “Diversity” in Nature

    Mammals have evolved two types of immunity: Innate and Specific. Both try to achieve the same goal i.e. elimination of any foreign infectious pathogen. Innate immunity is non-specific, in that it is not directed against a particular pathogen, but rather towards a common pattern, or a biomolecule, shared by many infectious agents. In case of bacteria, this may include their peptidoglycan Cell wall, or a membrane protein used in attaching bacterial Flagellum. The specific immunity, however, is towards a specific pathogen. One of the mediators of specific immunity is Immunoglobins. The latter comprises of IgG, IgM, IgA, IgE, IgD class. IgA is present in secretion, whether that be tears, breast milk, or digestive juices. IgM mediates the initial response against a pathogen, but IgG acts on any subsequent infections involving the same pathogen. On the other hand, IgE mediates allergic response, whereas IgD have no assigned function yet. In general, using IgG as an example, an Antibody consist of two heavy chains and two light chains. Using the disulfide bonds, not only the heavy chains are bound together, but the light chains are also attached to their respective heavy chain. In either a heavy chain or a light chain, there is further division. A heavy chain has VH1, CH1, CH2, CH3, whereas a light chain has VL1, CL1. VH1 and CH1 interacts with VL1 and CL1. C means constant region whereas V stands for variable region i.e. varying in amino acid sequence. It is the variability of VH1 and VL1 which assigns specificity to antibodies such that it can attach to, or rather tag, a particular antigen. These region makes up for the diversity in Antibodies. Just as there are different types of Seashells, there are different classes to Ig. Just as there are different patterns on one type of Seashell, there are different Antibodies in a class. The difference in Antibodies, belonging to a class, is because of their variability in amino acid sequence in VH1 and VL1 regions of Ig. This further implies that our body can synthesize thousands of different antibodies, and each one may bind to a completely different epitope, the site on antigen to which antibody attaches to. One of the mechanism behind such diversity in Ig seems to be Gene rearrangement. This means “Gene”, which encode for the VH1 and VL1, is segmented. And, these segments are randomly excised out, but, those intact are randomly combined to generate a completely different gene in process. Either way, once different types of Ig are generated, they lie dormant waiting for any foreign epitope to pass by.

    Reference/ Website for connection between my photo and prompt:
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3670108/

    Attachment:

Comments are closed.