Lecture21

Lecture21 - ecture 21 11/21/11 Background reading: Berg, et...

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Unformatted text preview: ecture 21 11/21/11 Background reading: Berg, et al: Pages 319 - 325 Garrett and Grisham: Pages 203 - 217 Outline: Analyses of results Use of recombinant DNA technology in protein purification Carbohydrates Monosaccharides Modifications of monosaccharides Oligosaccharides Analyses of results (continued) Electrophoresis: The most common type of electrophoresis is conducted using denaturing conditions in which SDS is added to disrupt noncovalent interactions and -mercaptoethanol is added to reduce disulfide bonds. The negative charge acquired by the protein by binding SDS is usually much greater than the charge on the native protein. The charge is roughly proportional to the mass of the protein. Smaller proteins will run faster than larger proteins through the gel. Isofocusing is often another electrophoretic technique used in the analysis of proteins. This technique separates the proteins on the basis of their isoelectric points. A pH gradient is constructed in a gel by using a variety of polyampholytes (small multicharged polymers) having many different pI values. The protein sample is then loaded to the gel and voltage is applied. The proteins will migrate to their isoelectric point in the gel. Use of recombinant DNA technology in protein purification The advent of recombinant DNA technology has enabled many proteins to be purified with greater ease using the following approaches. 1) Protein expression in a host organism that is amenable to genetic manipulation. Examples: E. coli Yeast Insect cells By exploiting the faster doubling times and genetic manipulation of such systems it is possible to obtain large amounts of protein in a relatively faster time....
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This note was uploaded on 01/15/2012 for the course BIS 102 taught by Professor Hilt during the Fall '08 term at UC Davis.

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Lecture21 - ecture 21 11/21/11 Background reading: Berg, et...

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