Protein Biochemistry and Proteomics (The Experimenter by Hubert Rehm

By Hubert Rehm

Hubert Rehm's Protein Biochemistry and Proteomics is greater than a laboratory guide; it's a strategic consultant that offers the reader with information and tips for extra profitable lab experiments. utilizing a conversational but expert tone, Rehm presents an outline of numerous tools in protein biochemistry/proteomics. He presents brief and targeted summaries of regimen approaches in addition to listings of the benefits and downsides of other equipment. Readers will instantly experience that the writer if very accustomed to the demanding situations, and frustration of the day-by-day lab regimen. by no means earlier than has such a decent, tactical consultant been to be had for these undertaking lab experiments in the box of biochemistry.

  • Shows the right way to stay away from experimental lifeless ends and is helping clients enhance an intuition for the correct scan on the correct time
  • Contains brief and detailed summaries of regimen strategies (e.g. column chromatography, gel electrophoresis), and lists the benefits and downsides of other methods
  • Includes over a hundred distinctive figures and tables
  • Contains a bankruptcy on proteomics

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Additional info for Protein Biochemistry and Proteomics (The Experimenter Series)

Sample text

HPLC is worth using if you iodine often, because after a run with 1 mCi 125iodine the 28 · 2 Ligand Binding machine cannot be used for cold work for at least one year. The HPLC is often able to distinguish between monoiodized and di-iodized peptides/proteins. For iodination reactions with good incorporation, you can skip separating the free 125iodine, especially because free 125iodine develops again during storage of the reaction product (back reaction). If you have to iodize a peptide that can withstand pH 3 and 100° C, you can iodize it fi rst with 127iodine.

The organic solvents denature some proteins even at low temperatures. Source 1. , and Seifter, S. (1990). “Precipitation Techniques,” Methods Enzymol. 182: 285–300. 3 Concentration Freeze-dry: Freeze-drying removes the water from frozen protein solutions by sublimation. You remember: in vacuum, ice does not change to water. Rather, the ice turns directly into steam (sublimation). Freeze-drying is typically done at RT (the solution remains frozen because sublimation continually channels energy away).

Proteins bind noncovalently to blot membranes. , for proteolytic digestion or for analysis in the MALDITOF). For nitrocellulose, Lui et al. (1996) have systematically examined the interaction of protein and blot membrane. According to them, Zwittergent 3–16 (1% in 100 mM NH4HCO3) removes between 60 and 90% of the blotted protein from the nitrocellulose. The detergent also works with PVDF membranes, albeit not as well. , Tween 20, Tween 80, hydrogenated TRITON-X-100) that remove proteins from the membrane.

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