Experiment 1-7 Lab report change Filtration Chromatography: Desalting of a protein containing firmness Group D: Viktorija Glembockyte and Laura Panavaite v.glembockyte@jacobs-university.de and l.panavaite@jacobs-university.de GRADE Jacobs University Bremen SIGNATURE 15/12/08 Experiment 1-7. mousse Filtration Chromatography: Desalting of a protein containing theme Introduction The biochemical characterization of an individual compound is all-important(a) for the understanding of this molecule’s function within the cell. such(prenominal) characterization do-nothing be performed only(prenominal) after polish of respective compound. Different properties of a biomolecule can be employ for the breakup. Proteins are usually isolated employ chromatographic techniques. In this experiment we used gel filtration chromatography – manner based withdrawal of molecules according to their size. Using this technique, BSA (Bovine Serum Albumin) was sepa rated from a solution containing it. Two different spectroscopic assays were carried erupt: the Bradford Assay and protein stopping point by absorbance measurement at 280 nm. These enabled us to identify and mensurate the BSA containing samples gained using gel chromatography separation technique (Illenberger et al., 2008).

Materials and Methods The experiments were carried out as described in the manual of arms with the following exceptions: in the photometrical analysis of gel fractions at 280 nm both samples were weaken twice to obtain dear absorption values smaller than 1 for higher accuracy. When tou chstone BSA absorbencies for the calibration! curve, all standards were lively twice, not once, therefore a mean value of cardinal different samples was used for obtaining apiece point of the calibration curve. For formulation of calibration standards 10 mg/mL BSA stock solution was used. 2 Experiment 1-7. Gel Filtration Chromatography: Desalting of a protein containing solution Results Gel filtration chromatography In the setoff bump of the...If you want to get a full essay, tack together it on our website:
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