Protein Purification
Quiz yourself by thinking what should be in
each of the black spaces below before clicking
on it to display the answer.
Help!
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| Gel filtration chromatography (size) | big molecules have a shorted path because they cannot fit trough, can only go around. medium is a bit longer. small is longest, can fit through so must go through all.
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| Dialysis | Semi-permeable membrane (excludes material at molecular level), Permeable (allows small molecules and water to pass), Impermeable (does not allow large molecules).
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| Dialysis | for rapid dialysis, maximise area of membrane/volume of solution.
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| SDS-page | Similar to electrophoresis but SDSP added to sample which applies a negative charge to each protein in proportion to its mass. SDS allows proteins to be separated strictly by molecular weight.
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| Silver stain | used to make invisible protein bands visible (BLACK)
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| Comassie blue | makes protein bands blue, less sensitive.
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| Mass spectrometry | Accurate reading of molecular weight, down to a single atom.
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| Cation-exchange chromatography | Has -vely charged polymer beads. Rate of movement determined by net charge at the pH used. More -ve proteins move faster because like charges repel.
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| Isoelectric focussing IEF | Charge on a protein is affected by pH. A pH gradient is set up and an electric current is passed through. When protein reached pI, it stops.
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| 2D-PAGE | first dimension = IEF, separation by charge. second dimension = SDS-PAGE, separation by size. decreasing Mr vertically, decreasing pI horizontally.
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Created by:
nyna
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