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WorldOfBiochemistry

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About WorldOfBiochemistry

  • Rank
    Quark
  • Birthday 01/12/1980

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    http://worldofbiochemistry.blogspot.com/

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  • Location
    Portugal
  • College Major/Degree
    PhD
  • Favorite Area of Science
    Biochemistry
  • Occupation
    College professor
  1. I am not sure, but probably you will get some useful information in textbooks about cancer's biology... Good luck!
  2. I don't know if I understood correctly your question, but you can measure glucose by quantifying the activity og glucose-6-phosphate dehydrogenase, for example. However, pçlease keep in mind that if you need to collect blood and the analysis is not performed imediately after collection, you will need to stop glycolisis. Fluoride, EDTA or citrate will work fine for that.
  3. Hi Ghaz, unfortunately there are many reasons that can justify the lack of activity of an eukaryotic protein produced by bacteria. Some of the most recurrent problems are: 1. Absence of post-translational modifications in the producing cell 2. Absence of chaperones suitable for a proper folding of the protein 3. Non-specific interactions with host proteins and/or other molecules 4. Structure alterations due to lab manipulations during the isolation and purification of the protein 5. (...)
  4. Hi, you should try to perform the search in PubMed: http://www.ncbi.nlm.nih.gov/ Good luck!
  5. I don't have experience in measuring lysozyme, but probably you will find elisa kits for that (try abcam and/or r&d systems). Alternatively, try to find if there is any enzymatic assay for lysozyme. Probably it will be less expensive...
  6. Hi, I have never seen something like that. Are the cells alive or fixed?
  7. Hi Green Xenon, I don't think it will be possible to have those molecules as products of fermentation. Probably you will get some as metabolic intermediates in the catabolism of aminoacids, for example, but not fermentation.
  8. I usually buy the chemicals to Sigma-Aldrich or Merck. Those are the two most widely known brands...
  9. The best way is to check if the information is supported by scientific literature. That means that in the text there must be references to the scientific papers/books where the information was retrieved.
  10. I agree, but the problem was that after they put sodium in the pipes, they add some water through them.
  11. Hi alphas, in fact your results are a bit strange. Probably the polimerization did not occur in a homogeneous way, wich created some pH gradients... I am sorry but unfortunately I can not help you much more than this... Have you checked Maniatis book, the "bible" of Molecular Biology, to see if it contains any help?
  12. What about your protein bands. Do they also disappear?
  13. I agree. Watching TV and watching computer might not be the same thing, because TV is a more "passive" activity, with might stimulate less our brain. Nevertheless, both pose some health risks.
  14. pH and temperature can "clean" solutions, if they are in the correct values.
  15. Hi, before you start to analyse a pecific bond, there are some general rules that can easier your work. 1 - All aminoacids have at least a carboxylic and an amine group. Since they are polar groups, that can establish polar bonds with other aminoacids. That is, dipole-dipole bonds. Moreover, once they have very electronegative atoms and hydrogens bonded to them, they can establish hydrogen bonds. Also, they are ionizable, which means that they also might establish ionic bridges. 2 - Each aminoacid have a specific lateral group that may be hydrophobic, polar (uncharged) and polar (charged). Hydrophobic groups establish hydrophobic interactions with other hydrophobic groups. Polar (uncharged) establish dipole-dipole bonds (in some cases hydrogen bonds, that is a specific type of dipole-dipole bonds). Polar (charged) establish the same as the polar (uncharged) plus salt bridges. Thus, what I recommend you is to divide the aminoacids in groups accordingly the chemical properties of the lateral groups. Then is just necessary to apply the rules that I have mentioned before. In respect to covalent bonds between aminoacids, the most common are peptide bonds and disulphide bonds.
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