365 S2011 L8 - Midterm 1! high 100! low 26! mean 70! 1...

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1 Midterm 1 high 100 low 26 mean 70
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6 • Which fractions contains the protein of interest? • Was this a good technique to do? Protein puriFcation, trial and error
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7 Bookkeeping 1. Specifc activity = total activity/amount oF protein 2. Yield = activity aFter/activity beFore 3. ±old purifcation = specifc activity aFter/specifc activity beFore
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8 Yield Specifc activity Fold purifcation Evaluation o± a step in the purifcation
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9 Separation techniques
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10 Salting out • Protein solubility is mediated by polar groups on its surface • Ions compete with proteins for solvent molecules • (NH4) 2 SO 4 precipitation
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11 Salting out (NH4) 2 SO 4
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12 Chromatography Discovered in 1903 to separate pigments present in plants
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13 Column chromatography 1 Ion-exchange — charge 2 Hydrophobic interaction — hydrophobicity 3 Gel-fltration — size 4 AFfnity — specifc interaction
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14 Ion-exchange Charged molecules bind to opposite charged groups on the column – Anion exchange (DEAE) – Cation exchange (CM) • AfFnity depends on the presence of salt and the pH
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This note was uploaded on 05/07/2011 for the course CHEM 365 taught by Professor Huxford during the Spring '08 term at San Diego State.

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365 S2011 L8 - Midterm 1! high 100! low 26! mean 70! 1...

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