While the tube for specimen Cb turned a tannish white in the lower half of the tube while the top stayed the lavender inoculated tube color. Do to this evidence I determined that both specimens Ca and Cb cannot use the process Casein hydrolysis or Casein coagulation due to lack of soft or firm curds in both tubes. Since there was no casein curds formed, I concluded that specimens Ca and Cb also cannot perform the process of proteolysis. My conclusion is supported by the fact that there was no clearing of the medium. I have also determine that neither of my organisms can make the enzymes rennin, proteolytic or even proteases. I know my specimens cannot produce proteases due to the fact that there was no blue coloring in the tubes which means that the byproduct Ammonia was not produced to increase the pH. Since neither of my specimens can make these enzymes, I concluded that my specimens cannot break down lactose or casein. Although I did learn that specimen Cb can reduce litmus due to the evidence that the lower part of the tube turned a tannish white color with a purple ring at the top. This color change from a purple to a white means that the litmus was reduced turning it clear and leaving the white of the milk to show. Finally I know that specimen Ca cannot reduce litmus due to the fact that the tube had no change in
...ubunit structure of the protein . The damage caused due to radioiodination was experimentally proved by isoelectric focusing studies . When conditions for reagent concentration was optimized, ideally for every one molecule of oxidant two molecules of reductant is needed to stop the reaction. The result was consistent with the previous radioiodination techniques studied for different protein molecules. It was demonstrated that when incubation time was increased it resulted in damage to the protein. The damage might have caused probably due to increased time of exposure of active iodide species with the protein. Studies on the effect of temperature gave yield of 75% when the reaction was performed at 2oC which is supported by the conclusion that at ambient temperature labeled BSA is in an aggregated form which lowers the iodination yield at low temperature .
...n phases and titer relationship, as well as to show that the 1:2 dilutions of the anti-ova antibody produce an exponential (curved) decrease of the OD of the anti-ova antibody as the 1:2 dilutions increase. However, day 21, when the anti-ova antibody titer is at the greatest OD, the first initial dilutions of the anti-ova antibody have no effect on the on the OD which means that the OD is so high, and there is so much anti-ova antibody, that diluting the antibody did not have an effect on the OD. After the 1:800 dilution, the OD begins to decrease exponentially but less sharply than day 2, 14, and 28 thus serving the purpose of the dilution analyses. The data that was collected for this experiment was consistent with the stated hypothesis. The days that had the highest titer, days 14 and 21, were predicted in the hypothesis and were confirmed by the collected data.
...at keep organisms alive. “Proteins are the most structurally sophisticated molecules known” (Campbell, 1999) which is reason enough to study them. The techniques we learned in this lab form a basis from which a detailed study of proteins is possible. Following our procedure we were successfully able to set up a quantifying assay to determine the amount of protein within a milk sample, although our yield percentage was rather low. However, errors in this lab (in the form of a low yield percentage) may have an origin from our last lab. In the process of extracting proteins from the milk sample, we may have inadvertently lost some of the protein through erroneous measurements, or perhaps through poor handling of either ammonium sulfate or the dialysis tubing. While not sufficient enough (at this point) to invalidate our results, they do explain the major difference between the expected and the actual amount of protein extracted.
...t. The binding potential of a specific antibody is greatly expanded by the ability of germ line antibodies to undergo further mutation and adopt more than one combining-site configuration. The results imply that there is an entirely new level of antigen recognition that takes place after the germ line antibody has bound to its antigen, and that this new level of recognition significantly increases the binding potential and effectiveness of the antibody.
Transfected cells were lysed, lysates were immunoprecipitated by anti-flag or anti-HA antibody (Sigma, USA) and the immunoprecipitates were captured by an overnight incubation with protein G sepharose beads (GE healthcare, USA) which was followed by 3 times washing of beads in lysis buffer. Standard western blotting was done on the immunoprecipitated proteins. The primary antibodies that were used in this study are: anti-flag (Sigma, USA), anti-EVI1 (Cell Signalling, USA), and anti-HA (Roche, Switzerland). Secondary HRP conjugated antibodies raised ...
... amino acid changes which increase the tightness of binding of the antibody on the B cell to its antigen. These B cells will compete more efficiently for antigen than the original B cell, and will differentiate into plasma cells producing a higher-affinity antibody (affinity maturation), resulting increase of affinity to the antibody population to that antigen. After successive immunization, antibodies have binding constants of 108-9 M-1 but may be as high as 1012 M-1.
The radioallergosorbent test (RAST) is an RIA test that allows for the detection and quantification of IgE antibodies. During the test, a possible allergen is bound to insoluble material and a sample of the patient’s blood is added. If the blood sample contains antibodies specific to that allergen, the antibodies will bind to that allergen. Anti-human radiolabeled IgE antibodies are then added and bind only to the antibodies already bound to the insoluble material. The whole sample is then wThe unbound anti-human antibodies are washed away and the level of radioactivity is proportional to the amount of human IgE present in the blood sample.